Relevant bibliographies by topics / Membrane bound proteins

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Membrane bound proteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Membrane bound proteins"

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Nishikiori, Masaki, Koji Dohi, Masashi Mori, Tetsuo Meshi, Satoshi Naito, and Masayuki Ishikawa. "Membrane-Bound Tomato Mosaic Virus Replication Proteins Participate in RNA Synthesis and Are Associated with Host Proteins in a Pattern Distinct from Those That Are Not Membrane Bound." Journal of Virology 80, no. 17 (September 1, 2006): 8459–68. http://dx.doi.org/10.1128/jvi.00545-06.

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ABSTRACT Extracts of vacuole-depleted, tomato mosaic virus (ToMV)-infected plant protoplasts contained an RNA-dependent RNA polymerase (RdRp) that utilized an endogenous template to synthesize ToMV-related positive-strand RNAs in a pattern similar to that observed in vivo. Despite the fact that only minor fractions of the ToMV 130- and 180-kDa replication proteins were associated with membranes, the RdRp activity was exclusively associated with membranes. A genome-sized, negative-strand RNA template was associated with membranes and was resistant to micrococcal nuclease unless treated with detergents. Non-membrane-bound replication proteins did not exhibit RdRp activity, even in the presence of ToMV RNA. While the non-membrane-bound replication proteins remained soluble after treatment with Triton X-100, the same treatment made the membrane-bound replication proteins in a form that precipitated upon low-speed centrifugation. On the other hand, the detergent lysophosphatidylcholine (LPC) efficiently solubilized the membrane-bound replication proteins. Upon LPC treatment, the endogenous template-dependent RdRp activity was reduced and exogenous ToMV RNA template-dependent RdRp activity appeared instead. This activity, as well as the viral 130-kDa protein and the host proteins Hsp70, eukaryotic translation elongation factor 1A (eEF1A), TOM1, and TOM2A copurified with FLAG-tagged viral 180-kDa protein from LPC-solubilized membranes. In contrast, Hsp70 and only small amounts of the 130-kDa protein and eEF1A copurified with FLAG-tagged non-membrane-bound 180-kDa protein. These results suggest that the viral replication proteins are associated with the intracellular membranes harboring TOM1 and TOM2A and that this association is important for RdRp activity. Self-association of the viral replication proteins and their association with other host proteins may also be important for RdRp activity.
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YAMAMOTO, Eiji. "Interaction of Membrane Bound Proteins with Phosphoinositide-containing Membranes." Seibutsu Butsuri 61, no. 4 (2021): 253–54. http://dx.doi.org/10.2142/biophys.61.253.

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ARGOS, Patrick, J. K. Mohana RAO, and Paul A. HARGRAVE. "Structural Prediction of Membrane-Bound Proteins." European Journal of Biochemistry 128, no. 2-3 (March 3, 2005): 565–75. http://dx.doi.org/10.1111/j.1432-1033.1982.tb07002.x.

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Ulbrich, Maximilian H., and Ehud Y. Isacoff. "Subunit counting in membrane-bound proteins." Nature Methods 4, no. 4 (March 18, 2007): 319–21. http://dx.doi.org/10.1038/nmeth1024.

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Rosiere, T. K., J. A. Marrs, and G. B. Bouck. "A 39-kD plasma membrane protein (IP39) is an anchor for the unusual membrane skeleton of Euglena gracilis." Journal of Cell Biology 110, no. 4 (April 1, 1990): 1077–88. http://dx.doi.org/10.1083/jcb.110.4.1077.

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The major integral plasma membrane protein (IP39) of Euglena gracilis was radiolabeled, peptide mapped, and dissected with proteases to identify cytoplasmic domains that bind and anchor proteins of the cell surface. When plasma membranes were radioiodinated and extracted with octyl glucoside, 98% of the extracted label was found in IP39 or the 68- and 110-kD oligomers of IP39. The octyl glucoside extracts were incubated with unlabeled cell surface proteins immobilized on nitrocellulose (overlays). Radiolabel from the membrane extract bound one (80 kD) of the two (80 and 86 kD) major membrane skeletal protein bands. Resolubilization of the bound label yielded a radiolabeled polypeptide identical in Mr to IP39. Intact plasma membranes were also digested with papain before or after radioiodination, thereby producing a cytoplasmically truncated IP39. The octyl glucoside extract of truncated IP39 no longer bound to the 80-kD membrane skeletal protein in the nitrocellulose overlays. EM of intact or trypsin digested plasma membranes incubated with membrane skeletal proteins under stringent conditions similar to those used in the nitrocellulose overlays revealed a partially reformed membrane skeletal layer. Little evidence of a membrane skeletal layer was found, however, when plasma membranes were predigested with papain before reassociation. A candidate 80-kD binding domain of IP39 has been tentatively identified as a peptide fragment that was present after trypsin digestion of plasma membranes, but was absent after papain digestion in two-dimensional peptide maps of IP39. Together, these data suggest that the unique peripheral membrane skeleton of Euglena binds to the plasma membrane through noncovalent interactions between the major 80-kD membrane skeletal protein and a small, papain sensitive cytoplasmic domain of IP39. Other (62, 51, and 25 kD) quantitatively minor peripheral proteins also interact with IP39 on the nitrocellulose overlays, and the possible significance of this binding is discussed.
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Stochaj, W. R., T. Berkelman, and N. Laird. "Staining Membrane-Bound Proteins with Ponceau S." Cold Spring Harbor Protocols 2006, no. 28 (October 1, 2006): pdb.prot4543. http://dx.doi.org/10.1101/pdb.prot4543.

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Stochaj, W. R., T. Berkelman, and N. Laird. "Staining Membrane-Bound Proteins with Colloidal Gold." Cold Spring Harbor Protocols 2006, no. 28 (October 1, 2006): pdb.prot4545. http://dx.doi.org/10.1101/pdb.prot4545.

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Sapp, Kayla, and Lutz Maibaum. "Fluctuation-Induced Interactions between Membrane-Bound Proteins." Biophysical Journal 108, no. 2 (January 2015): 543a. http://dx.doi.org/10.1016/j.bpj.2014.11.2980.

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Bilodeau, Diane, Sylvie Lamy, Richard R. Desrosiers, Denis Gingras, and Richard Béliveau. "Regulation of Rho protein binding to membranes by rhoGDI: inhibition of releasing activity by physiological ionic conditions." Biochemistry and Cell Biology 77, no. 1 (March 1, 1999): 59–69. http://dx.doi.org/10.1139/o99-004.

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The Rho GDP dissociation inhibitor (GDI) is an ubiquitously expressed regulatory protein involved in the cycling of Rho proteins between membrane-bound and soluble forms. Here, we characterized the Rho solubilization activity of a glutathione S-transferase (GST) - GDI fusion protein in a cell-free system derived from rat kidney. Addition of GST-GDI to kidney brush border membranes resulted in the specific release of Cdc42 and RhoA from the membranes, while RhoB and Ras were not extracted. The release of Cdc42 and RhoA by GST-GDI was dose dependent and saturable with about 50% of both RhoA and Cdc42 extracted. The unextracted Rho proteins were tightly bound to membranes and could not be solubilized by repeated GST-GDI treatment. These results demonstrated that kidney brush border membranes contained two populations of RhoA and Cdc42. Furthermore, the GST-GDI solubilizing activity on membrane-bound Cdc42 and RhoA was abolished at physiological conditions of salt and temperature in all tissues examined. When using bead-immobilized GST-GDI, KCl did not reduced the binding of Rho proteins. However, washing brush border membranes with KCl prior treatment by GST-GDI inhibited the extraction of Rho proteins. Taken together, these results suggest that the binding of GDI to membrane-bound Cdc42 and RhoA occurs easily under physiological ionic strength conditions, but a complementary factor is required to extract these proteins from membranes. These observations suggest that the shuttling activity of GDI upon Rho proteins could be normally downregulated under physiological conditions.Key words: rhoGDI, rho proteins, ionic strength, kidney.
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Harder, T., R. Kellner, R. G. Parton, and J. Gruenberg. "Specific release of membrane-bound annexin II and cortical cytoskeletal elements by sequestration of membrane cholesterol." Molecular Biology of the Cell 8, no. 3 (March 1997): 533–45. http://dx.doi.org/10.1091/mbc.8.3.533.

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Annexin II is an abundant protein which is present in the cytosol and on the cytoplasmic face of plasma membrane and early endosomes. It is generally believed that this association occurs via Ca(2+)-dependent binding to lipids, a mechanism typical for the annexin protein family. Although previous studies have shown that annexin II is involved in early endosome dynamics and organization, the precise biological role of the protein is unknown. In this study, we found that approximately 50% of the total cellular annexin was associated with membranes in a Ca(2+)-independent manner. This binding was extremely tight, since it resisted high salt and, to some extent, high pH treatments. We found, however, that membrane-associated annexin II could be quantitatively released by low concentrations of the cholesterol-sequestering agents filipin and digitonin. Both treatments released an identical and limited set of proteins but had no effects on other membrane-associated proteins. Among the released proteins, we identified, in addition to annexin II itself, the cortical cytoskeletal proteins alpha-actinin, ezrin and moesin, and membrane-associated actin. Our biochemical and immunological observations indicate that these proteins are part of a complex containing annexin II and that stability of the complex is sensitive to cholesterol sequestering agents. Since annexin II is tightly membrane-associated in a cholesterol-dependent manner, and since it seems to interact physically with elements of the cortical actin cytoskeleton, we propose that the protein serves as interface between membranes containing high amounts of cholesterol and the actin cytoskeleton.
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Dissertations / Theses on the topic "Membrane bound proteins"

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Whitehead, L. "Computer simulation of biological membranes and membrane bound proteins." Thesis, University of Southampton, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.297412.

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Adcock, Stewart Alan. "Computer simulation of membrane bound molecules." Thesis, University of Oxford, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249194.

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Höglund, Pär J. "Identification, Characterization and Evolution of Membrane-bound Proteins /." Uppsala : Acta Universitatis Upsaliensis Acta Universitatis Upsaliensis, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-9329.

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Höglund, Pär J. "Identification, Characterization and Evolution of Membrane-bound Proteins." Doctoral thesis, Uppsala universitet, Institutionen för neurovetenskap, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-9329.

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Membrane proteins constitute approximately 30% of all genes in the human genome and two large families of membrane proteins are G protein-coupled receptors (GPCRs) and Solute Carriers (SLCs) with about 800 and 380 human genes, respectively. In Papers I, II and IV, we report 16 novel human Adhesion GPCRs found by searches in NCBI and Celera databases. In Paper I, we report eight novel human GPCRs, and six in Paper II. We identified two new human Adhesion GPCRs and 17 mouse orthologs in Paper IV. Phylogenetic analysis demonstrates that the 16 novel human genes are additional members of the Adhesion GPCR family and can be divided into eight phylogenetic groups. EST expression charts for the entire repertoire of Adhesions in human and mouse were established, showing widespread distribution in both central and peripheral tissues. Different domains were found in their N-terminus, some, such as pentraxin in GPR112, indicates that they take part in immunological processes. In Paper III, we discovered seven new human Rhodopsin GPCRs. In Paper V, we present the identification of two new human genes, termed SLC6A17 and SLC6A18 from the Solute Carriers family 6 (SLC6). We also identified the corresponding orthologs and additional genes from the mouse and rat genomes. We analysed, in total, 430 unique SLC6 proteins from 10 animal, one plant, two fungi and 196 bacterial genomes. In Paper VI, we provide the first systematic analysis of the evolutionary history of the different SLC families in Eukaryotes. In all, we analysed 2403 sequences in eight species and we delineate the evolutionary history of each of the 46 SLC families.
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Chandler, Becky. "Interrelationships between HIV, antiretroviral therapy and membrane bound proteins." Thesis, University of Liverpool, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.402412.

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Witkowski, Thomas, Rainer Backofen, and Axel Voigt. "The influence of membrane bound proteins on phase separation and coarsening in cell membranes." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2014. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-139226.

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A theoretical explanation of the existence of lipid rafts in cell membranes remains a topic of lively debate. Large, micrometer sized rafts are readily observed in artificial membranes and can be explained using thermodynamic models for phase separation and coarsening. In live cells such domains are not observed and various models are proposed to describe why the systems do not coarsen. We review these attempts critically and show within a phase field approach that membrane bound proteins have the potential to explain the different behaviour observed in vitro and in vivo. Large scale simulations are performed to compute scaling laws and size distribution functions under the influence of membrane bound proteins and to observe a significant slow down of the domain coarsening at longer times and a breakdown of the self-similarity of the size-distribution function
Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich
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Witkowski, Thomas, Rainer Backofen, and Axel Voigt. "The influence of membrane bound proteins on phase separation and coarsening in cell membranes." Royal Society of Chemistry, 2012. https://tud.qucosa.de/id/qucosa%3A27814.

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A theoretical explanation of the existence of lipid rafts in cell membranes remains a topic of lively debate. Large, micrometer sized rafts are readily observed in artificial membranes and can be explained using thermodynamic models for phase separation and coarsening. In live cells such domains are not observed and various models are proposed to describe why the systems do not coarsen. We review these attempts critically and show within a phase field approach that membrane bound proteins have the potential to explain the different behaviour observed in vitro and in vivo. Large scale simulations are performed to compute scaling laws and size distribution functions under the influence of membrane bound proteins and to observe a significant slow down of the domain coarsening at longer times and a breakdown of the self-similarity of the size-distribution function.
Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich.
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O'Ryan, Liam. "Studies on the structure of membrane bound and membrane associated proteins using scattering techniques." Thesis, University of Manchester, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.518435.

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Doughty, Stephen William. "Molecular modelling of voltage-gated calcium channels." Thesis, University of Oxford, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362014.

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Ladomery, Michael R. "Analysis of proteins bound to stored messenger RNA in Xenopus oocytes." Thesis, University of St Andrews, 1996. http://hdl.handle.net/10023/14505.

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Regulation at the post-transcriptional level is gaining significance at a rapid pace. One example is the storage of messenger mRNA molecules in a translationally quiescent state, the so-called "masked messengers". Their existence has been known since the 1960s, but many details of their composition and structure have not yet been resolved. Masked messenger RNAs are particularly abundant in the oocytes of the African clawed toad Xenopus laevis. The aim of this study has been to examine the proteins bound to stored mRNAs in the oocytes, by focussing on the Y-box proteins which had already been identified as major components in mRNA masking, and by analyzing some of the other unidentified mRNP proteins. The YB proteins were studied in greater detail, gaining fresh information about their RNA-binding properties, defining distinct binding domains. The presence of an mRNP-associated protein kinase was confirmed, and binding assays suggested that phosphorylation influences the ability of the YB proteins to bind to mRNA. cDNA expression libraries were screened both with an RNA-binding assay and with an immunoscreening method, isolating a variety of known and novel cDNAs. Peptide sequencing of mRNP proteins revealed the presence of an RNA helicase distinct from the translation initiation factor eIF4A. It is postulated that the RNA helicase, in addition to the YB proteins, will be seen to have an important role in the formation and activity of the masked messenger RNA particles.
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Books on the topic "Membrane bound proteins"

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Lattman, Eaton E., Thomas D. Grant, and Edward H. Snell. Distinct Instrumental Approaches to SAXS. Oxford University Press, 2018. http://dx.doi.org/10.1093/oso/9780199670871.003.0010.

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There are more specialized applications of SAXS and SANS which require specific experimental considerations. This chapter covers size exclusion chromatography which has proven to be useful to study both soluble and membrane bound proteins allowing the study of samples that show time and concentration dependent dynamics. It also describes iime-resolved techniques for SAXS and in a few cases, SANS. Finally, with improved X-ray sources, detectors, sample handling, and compute power, the ability to perform SAXS data in high-throughput is available. This is discussed in enabling the use of SAXS to study protein interactions, map macromolecular conformation, and rapidly characterize samples amongst other applications.
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Murer, Heini, Jürg Biber, and Carsten A. Wagner. Phosphate homeostasis. Edited by Robert Unwin. Oxford University Press, 2015. http://dx.doi.org/10.1093/med/9780199592548.003.0025.

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Inorganic phosphate ions (H2PO4−/ HPO42−) (abbreviated as Pi) are involved in formation of bone and generation of high-energy bonds (e.g. ATP), metabolic pathways, and regulation of cellular functions. In addition, Pi is a component of biological membranes and nucleic acids. Only about 1% of total body Pi content is present in extracellular fluids, at a plasma concentration in adults within the range 0.8–1.4 mMol/L (at pH 7.4 mostly as HPO42−), with diurnal variations of approximately 0.2 mM. A small amount of plasma Pi is bound to proteins or forms complexes with calcium. Under normal, balanced conditions, absorption of dietary Pi along the small intestine equals the output of Pi via kidney and faeces. Renal excretion of Pi represents the key determinant for the adjustment of normal Pi plasma concentrations. Renal reabsorption of Pi occurs along the proximal tubules by sodium-dependent Pi cotransporters that are strictly localized at the apical brush border membrane. Parathyroid hormone (PTH) and FGF23 are key regulators amongst a myriad of factors controlling excretion of Pi in urine, mostly by changes of the apical abundance of Na/Pi cotransporters. Hypophosphataemia may result in osteomalacia, rickets, muscle weakness, and haemolysis. Hyperphosphataemia can lead to hyperparathyroidism and severe calcifications in different tissues.
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Alexander, D. J., N. Phin, and M. Zuckerman. Influenza. Edited by I. H. Brown. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198570028.003.0037.

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Influenza is a highly infectious, acute illness which has affected humans and animals since ancient times. Influenza viruses form the Orthomyxoviridae family and are grouped into types A, B, and C on the basis of the antigenic nature of the internal nucleocapsid or the matrix protein. Infl uenza A viruses infect a large variety of animal species, including humans, pigs, horses, sea mammals, and birds, occasionally producing devastating pandemics in humans, such as in 1918 when it has been estimated that between 50–100 million deaths occurred worldwide.There are two important viral surface glycoproteins, the haemagglutinin (HA) and neuraminidase (NA). The HA binds to sialic acid receptors on the membrane of host cells and is the primary antigen against which a host’s antibody response is targeted. The NA cleaves the sialic acid bond attaching new viral particles to the cell membrane of host cells allowing their release. The NA is also the target of the neuraminidase inhibitor class of antiviral agents that include oseltamivir and zanamivir and newer agents such as peramivir. Both these glycoproteins are important antigens for inducing protective immunity in the host and therefore show the greatest variation.Influenza A viruses are classified into 16 antigenically distinct HA (H1–16) and 9 NA subtypes (N1–9). Although viruses of relatively few subtype combinations have been isolated from mammalian species, all subtypes, in most combinations, have been isolated from birds. Each virus possesses one HA and one NA subtype.Last century, the sudden emergence of antigenically different strains in humans, termed antigenic shift, occurred on three occasions, 1918 (H1N1), 1957 (H2N2) and 1968 (H3N2), resulting in pandemics. The frequent epidemics that occur between the pandemics are as a result of gradual antigenic change in the prevalent virus, termed antigenic drift. Epidemics throughout the world occur in the human population due to infection with influenza A viruses, such as H1N1 and H3N2 subtypes, or with influenza B virus. Phylogenetic studies have led to the suggestion that aquatic birds that show no signs of disease could be the source of many influenza A viruses in other species. The 1918 H1N1 pandemic strain is thought to have arisen as a result of spontaneous mutations within an avian H1N1 virus. However, most pandemic strains, such as the 1957 H2N2, 1968 H3N2 and 2009 pandemic H1N1, are considered to have emerged by genetic re-assortment of the segmented RNA genome of the virus, with the avian and human influenza A viruses infecting the same host.Influenza viruses do not pass readily between humans and birds but transmission between humans and other animals has been demonstrated. This has led to the suggestion that the proposed reassortment of human and avian influenza viruses takes place in an intermediate animal with subsequent infection of the human population. Pigs have been considered the leading contender for the role of intermediary because they may serve as hosts for productive infections of both avian and human viruses, and there is good evidence that they have been involved in interspecies transmission of influenza viruses; particularly the spread of H1N1 viruses to humans. Apart from public health measures related to the rapid identification of cases and isolation. The main control measures for influenza virus infections in human populations involves immunization and antiviral prophylaxis or treatment.
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Book chapters on the topic "Membrane bound proteins"

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Baltscheffsky, M., and P. Nyrén. "Purification and Reconstitution of the Proton Translocating Membrane Bound Inorganic Pyrophosphatase from Rhodospirillum rubrum." In Membrane Proteins, 42–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-71543-3_5.

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Nishimura, Katsuyuki, Michikazu Tanio, and Satoru Tuzi. "Structure and Dynamics of Membrane-Bound Proteins." In Modern Magnetic Resonance, 1–13. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-28275-6_62-1.

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Nishimura, Katsuyuki, Michikazu Tanio, and Satoru Tuzi. "Structure and Dynamics of Membrane-Bound Proteins." In Modern Magnetic Resonance, 669–81. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-28388-3_62.

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Klare, Johann P., and Heinz-Jürgen Steinhoff. "Structural Information from Spin-Labelled Membrane-Bound Proteins." In Structural Information from Spin-Labels and Intrinsic Paramagnetic Centres in the Biosciences, 205–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/430_2012_88.

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Nanda, Hirsh. "Resolving Membrane-Bound Protein Orientation and Conformation by Neutron Reflectivity." In Proteins in Solution and at Interfaces, 99–111. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118523063.ch5.

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Shon, Ki-Joon, Patricia Schrader, Yongae Kim, Burkhard Bechinger, Michael Zasloff, and Stanley Opella. "NMR-Structural Studies of Membrane Bound Peptides and Proteins." In Biotechnology: Bridging Research and Applications, 109–24. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3456-9_8.

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Howe, Vicky, and Andrew J. Brown. "Determining the Topology of Membrane-Bound Proteins Using PEGylation." In Methods in Molecular Biology, 201–10. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6875-6_15.

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Ramesh, Adithya, and Ian Wheeldon. "Western Blotting of Membrane-Bound Proteins in Yarrowia lipolytica." In Methods in Molecular Biology, 233–47. New York, NY: Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1414-3_16.

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Allen, John F., and Michael A. Harrison. "Phosphorylation of Membrane Proteins in Control of Excitation Energy Transfer." In Molecular Biology of Membrane-Bound Complexes in Phototrophic Bacteria, 291–98. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4757-0893-6_34.

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Blumberg, W. E. "Fluorescence Energy Transfer as a Structural Probe in Membranes and Membrane-Bound Proteins." In Physical Methods on Biological Membranes and Their Model Systems, 95–122. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-7538-8_8.

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Conference papers on the topic "Membrane bound proteins"

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Lapetina, Eduardo G., Bryan R. Reep, and Luis Molina Y. Vedia. "NOVEL GTP-BINDING PROTEINS OF CYTOSOLIC AND MEMBRANE FRACTIONS OF HUMAN PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644629.

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We have assessed the binding of (α-32P)GTP to platelet proteins from cytosolic and membrane fractions. Proteins were separated by SDS-PAGE and electrophoretically transferred to nitrocellulose. Incubation of the nitrocellulose blots with (α-32p)GTP indicated the presence of specific and distinct GTP-binding proteins in cytosol and membranes. Binding was prevented by 10-100 nM GTP or GTPyS and by 100 nM GDP; binding was unaffected by 1 nM-1 μM ATP. One main GTP-binding protein (29.5 KDa) was detected in the membrane fraction while three others (29, 27, and 21 KDa) were detected in the soluble fraction. Two cytosolic GTP-binding proteins (29 and 27 KDa) were degraded by trypsin; another cytosolic protein (21 KDa) and the membrane-bound protein (29.5 KDa) were resistant to the action of trypsin. Treatment of intact platelets with trypsin or thrombin, followed by lysis and fractionation, did not affect the binding of (α-32P)GTP to the membrane-bound protein. GTPyS still stimulates phospholipase C in permeabilized platelets already preincubated with trypsin. This suggests that trypsin-resistant GTP-binding proteins might regulate phospholipase C stimulated by GTPyS. We have started to purify the membrane-bound, trypsin-resistant, GTP-binding protein. Purification includes 1 M NaCl extraction and the use of an FPLC system with successive phenyl superose and superose 12 columns.
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Harada, Harumi. "Subcellular localization of membrane bound proteins using SDS-FRL." In European Microscopy Congress 2020. Royal Microscopical Society, 2021. http://dx.doi.org/10.22443/rms.emc2020.899.

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Lapetina, Eduardo G. "THE ROLE OF INOSITIDES, PHOSPHOLIPASE C AND G-PROTEINS IN RECEPTOR TRANSDUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644775.

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It is now widely recognized that the activation of phospholipase C by specific agonists leads to the formation of two second messengers: (1) inositol trisphosphate, which releases Ca2+ from the endoplasmic reticulum to the cytosol and (2) 1,2- diacylglycerol, which stimulates protein kinase C. In the past few years, GTP-binding proteins have been associated with the regulation of phospholipase C. However, the identity of the GTP-binding protein involved and the type of association with phospholipase C is not yet known. It is now recognized that there are two types of phospholipase C enzymes: (a) a soluble enzyme that has been characterized in several tissues and does not preferentially hydrolyze polyphospholinositides and (b) membrane-bound enzymes that are coupled to the receptors, specifically hydrolyzing polyphosphoinositides and activated by membrane guanine nucleotide-binding proteins. Recent reports have tried to assess the involvement of GTP-binding proteins in the agonist-induced stimulation of phospholipase C, and various related aspects have been reported. These are concerned with: (a) detection of various GTP-binding proteins in platelets, (b) the effects of known inhibitors of GTP-binding proteins such as GDPgS or pertussis toxin on the agonist-induced stimulation of phospholipase C, (c) the direct effects of stimulators of GTP-binding proteins such as GTP, GTP-analogs and fluoride on phospholipase C activity, (d) the possible association of GTP-binding proteins to cytosolic phospholipase C that would then lead to degradation of the membrane-bound inositides and (e) cytosolic phospholipase C response to the activation of cell surface receptors. The emerging information has had contradictory conclusions. (1) Pretreatment of saponin-permeabilized platelets with pertussis toxin has been shown to enhance and to inhibit the thrombin-induced activation of phospholipase C. Therefore, it is not clear if a G protein that is affected by pertussis toxin in a manner similar to Gi or Go plays a central role in activation of phospholipase C. (2) Studies on the effect of GDPβ;S are also conflicting indicating that there may be GTP-independent and/or -dependent pathways for the activation of phosphoinositide hydrolysis. (3) A cytosolic phospholipase C is activated by GTP, and it has been advanced that this activity might trigger the hydrolysis of membrane-bound inositides. A cytosolic GTP-binding protein might be involved in this action, and it is speculated that an α-subunit might be released to the cytoplasm by a receptor-coupled mechanism to activate phospholipase C. However, no direct evidence exists to support this conclusion. Moreover, the exact contribution of phospholipase C from the membranes or the cytosol to inositide hydrolysis in response to cellular agonists and the relationship of those activites to membrane-bound or soluble GTP-binding proteins are unknown. Our results indicate that the stimulation of phospholipase C in platelets by GDPβS and thrombin are affected differently by GDPβS. GDPgSinhibits the formation of inositol phosphates produced by GTPγS but not that induced by thrombin. Thrombin, therefore, can directly stimulate phospholipase C without the involvement of a “stimulatory” GTP-binding protein, such as Gs, for the agonist stimulation of adenylate cyclase. However, an “inhibitory” GTP-binding protein might have some influence on thrombin-stimulated phospholipase C, since in the presence of GDPγS thrombin produces a more profound stimulation of phospholipase C.This “inhibitory” GTP-binding protein might be ADP-ribosylated by pertussis toxin because pertussis toxin can also enhance thrombin action on phospholipase C activity. Therefore, phospholipase C that responds to thrombin could be different from the one that responds to GTPγS. Cytosolic phospholipase C can be activated by GTP or GTP analogs, and the one that responds to thrombin should be coupled to the receptors present in the plasma membrane. The initial action of thrombin is to directly activate the plasma membrane-bound phospholipase C and the mechanism of this activation is probably related to the proteolytic action of thrombin or the activation of platelet proteases by thrombin. In agreement with this, trypsin can also directly activate platelet phospholipase C and, subsequently, GTPyS produces further activation of phospholipase C. If these two mechanisms are operative in platelets, the inhibition of cytosolic phospholipase C by GDPβS would allow a larger fraction of inositides for degradation of the thrombin-stimulated phospholipase C, as our results show.
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4

Yeo, E., B. C. Furie, and B. Furie. "PADGEM PROTEIN EXPRESSION IN HUMAN ERYTHROLEUKEMIA (HEL) CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643908.

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PADGEM (Platelet Activation-Dependent Granule ⇒ External Membrane) glycoprotein, a platelet alpha granule integral membrane protein with a molecular weight of 140,000, is translocated to the plasma membrane during granule secretion. PADGEM protein is expressed solely on activated platelets, but is not on the surface of resting platelets. Because HEL cells contain platelet alpha granule-like organelles and proteins (e.g. platelet factor 4, von Villebrands factor, β-thromboglobulin) and express certain platelet membrane proteins (e.g. GP IIb/IIIa, GPIb), we evaluated induced and uninduced HEL cells for the synthesis and expression of PADGEM protein. HEL cells were induced with 1.25% DMSO for 3-4 days, then grown in the absence of DMSO for 1-3 weeks. After eight cycles of DMSO exposure, the induced HEL cells were found to increase the expression of PADGEM, in contrast to the uninduced cells. Intact fixed and unfixed induced HEL cells were observed by immunofluorescence, utilizing KC4, a monoclonal anti-PADGEM antibody, to express PADGEM while non-induced HFT. cells expressed low levels of PADGEM. Both induced and uninduced HEL cells bound A2A9, an anti—GP Ilb/IIIa monoclonal antibody. Quantitative analysis by fluorescence activated cell sorting demonstrated a 2.5—fold increase in mean surface expression of PADGEM and 3.3—fold mean increase in GP IIb/IIIa surface expression compared to uninduced cells. By fluoresence microscopy, 70% of induced HEL cells expressed PADGEM protein versus 20% of the uninduced cells. GP-IIb/IIIa expression inoreased from 40% in noninduced cells to 90% in induced cells. The induced HEL cells contained PADGEM with a molecular weight identical to that of platelets, as demonstrated by Western blotting using the KC4 antibody. Direct binding experiments with 125I-KC4 antibody demonstrated that surface binding was specific, saturable, and time-dependent. Surface expression of PADGEM protein was not increased with platelet agonists (thrombin, epinephrine, ADP) nor cytokines (IL-1, IL-2, tissue necrosis factor). The surface density of PADGEM protein on induced HEL cells and activated platelets appears similar. HEL cells should provide a useful model to assist in the elucidation of the structure, function and biology of PADGEM protein.
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5

Kalyan, N. K., S. G. Lee, W.-T. Hum, R. Hartzell, M. Levner, and P. P. Hung. "IN VITRO STUDIES ON THE BINDING OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (t-PA) AND UROKINASE (u-PA) TO LIVER MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643603.

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The plasminogen activators, t-PA and u-PA, are glycoproteins known to be involved in homeostasis of the blood clotting system, and thus are of potential clinical use in the treatment of thrombosis. Several in vivo studies have shown that both t-PA and u-PA are quickly removed from the blood circulation, predominantly by the liver. The mechanism by which the liver removes these proteins is not understood. To delineate this, we conducted in vitro studies of binding of PAs or their derivatives to isolated mouse liver membranes utilizing a functional assay developed in our laboratory. The assay consisted of initial binding of t-PA to liver membranes followed by centrifugation to pellet the membranes and the assay of the activity of the membrane-bound t-PA by a fibrin-agar plate method. The bound t-PA, which retained complete enzymic activity, could be dissociated by SDS treatment in an undegraded form as shown by SDS-PAGE. The binding of t-PA as well as u-PA was very fast and did not compete with glycoproteins or sugars containing the terminal galactose, mannose and N-acetylglucosamine residues. Furthermore, the treatment of t-PA with neuraminidase and/or periodate oxidation did not affect its binding characteristics. These data suggest that the carbohydrate moieties of t-PA and u-PA, unlike many glycoproteins, do not mediate their binding to the liver. This raised the possibility of the liver binding sequence being located in the protein backbone, especially the non-protease domains which are known to determine the biological specificities of PAs. The relative binding of u-PA and its low molecular weight (LMW) derivative containing only the protease domain, to the liver membranes was studied. Unlike u-PA and t-PA, LMW-urokinase did not bind significantly. This suggests that the protein sequence containing the non-protease domains, rather than the carbohydrate moieties of PAs contain the information necessary for binding to the liver and possibly their clearance from the blood circulation.
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6

Taylor, Graham, Donald Leo, and Andy Sarles. "Detection of Botulinum Neurotoxin/A Insertion Using an Encapsulated Interface Bilayer." In ASME 2012 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. American Society of Mechanical Engineers, 2012. http://dx.doi.org/10.1115/smasis2012-8101.

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Many signaling mechanisms in living cells occur at biological boundaries via cell surface receptors and membrane proteins embedded in lipid bilayers. The coordination of actions of sensory and motor neurons in the nervous system represents one example of many that heavily depends on lipid membrane bound receptor mediated signaling. As a result, chemical and biological toxins that disrupt these neural signals can have severe physiological effects, including paralysis and death. Botulinum neurotoxin Type A (BoNT/A) is a proteolytic toxin that inserts through vesicle membranes and cleaves membrane receptors involved with synaptic acetylcholine uptake and nervous system signal conduction. In this work, we investigate the use of a Bioinspired liquid-supported interface bilayer for studying the insertion of BoNT/A toxin molecules into synthetic lipid bilayers. DPhPC lipid bilayers are formed using the regulated attachment method (RAM), as developed by Sarles and Leo, and we perform current measurements on membranes exposed to BoNT/A toxin to characterize activity of toxin interacting with the synthetic bilayer. Control tests without toxin present are also presented. The results of these tests show an increase in the magnitude of current through the bilayer when the toxin is included. We interpret these initial results to mean that incorporation of BoNT/A toxin at a high concentration in an interface bilayer increases the permeability of the membrane as a result of toxin molecules spanning the thickness of the bilayer.
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7

Hirai, K., K. Yasunaga, and R. Ryo. "STUDIES ON PLATELET ANTIGENS AGAINST SERA FROM PATIENTS WITH ITP." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644583.

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Chronic idiopathic thrombocytopenic purpura (ITP) is a clinical syndrome characterized by destruction of platelets by antiplatelet antiboodies. The precise pathogenic mechanism of platelet destruction in ITP is not known, although many investigators have reported that platelet-associated IgG (PAIgG) is increased in this desease. We have evaluated PAIgG in 66 patients with ITP by a competitive solidphase microenzyme immunoassay and investigated its specificity aganist antiplatelet antibody in 24 patients with ITP by Western blotting. PAIgG values were elevated in most ITP patients with platelet counts of under 50,000/μl, but within normal range in most patients with platelet count of over 50,000/μl. PAIgG values were also elevated in ITP patients with megakaryocyte counts of over 200/μl, and within normal range in most patients with normal megakaryocyte counts. Western blotting was carried out by SDS-PAGE of whole platelet lysate or platelet membrane lysate and trasfer of the platelet fraction onto nitrocellulose strips. Bound immunoglobulins were detected with an avidin-biotin-peroxidase system. Several bands of bound immunoglobulins were detected in the whole platelet lysates of ITP patients, but most of these could not be detected in platelet membrane lysates. This finding suggests that some immunoglobulins from ITP patients may bind to cytoplasmic proteins in whole platelet lysate. These observations are consistent with the hypothesis that the pathogenesis of ITP involves an immunological mechanism.
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8

Simone, E. R., T. A. Davies, N. A. Zabe, S. M. Greenberg-seperaky, and N. E. Larsen. "EARLY PLATELET-THROMBIN RECEPTORS AND THEIR FUNCTIONS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643730.

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Human platelets possess less than 1000 high affinity [Kd=10-9]and 50-100,000 receptors of lower [Kd=10-7] affinity for o(α-thrombin. The selective derivatization of thrombin with the bifunctional crosslinking agent, DNCO, has enabled us to identify these receptorsvia covalent binding of either active siteinhibited tosyllyslmethylketothrombin (TLCK-T) or active Ctf-thrombin (T).Kinetic studies of the inhibition of the platelet-thrombin response by covalently and noncovalently bound TLCK-T have helped to elucidate the roles of the high and low affinity thrombin receptors. The activation parameters examined were initial membrane depolarization, cytoplasmic alkalinization,dense granule secretion of serotonin and lysosomal secretion of β-glucuronidase.Isolation and characterization of the thrombin receptors after covalent photocoupling of the TLCK-T or active T- were performed after solubilization by gel filtration. The intact, high affinity receptor moiety, a glycoprotein, has an approximate molecular weight of∽lSO.OOO daltons; occasionally this protein is found as a dimer of ∽360,000 daltons. When exposed to o(α-T the receptor undergoes proteolysis, leaving a protein of∽80,000 daltons and releasing the remaining glycoprotein into the medium.Higher doses of active T have been shown to bind with lower affinity to a larger protein of approximate molecular weight 600,000 daltons anda smaller protein of 46,000 daltons. Both proteins are nonsusceptible to thrombin proteolysis. Reduction and alkylation of the600,000 dalton complex yielded two and possibly three high molecular weight components (200,000, 160,000, and possibly 145,000daltons) which may correspond to previously suggested GP-Ia and GP-Ib of the GP-I complex. Under different solubilization conditions, two other membrane proteins have been found to be part of the GP-I complex; one which is not a glycoprotein, GP-Ic, while the other is associated with the glycocalyx and is called glycocalicin. Glycocalicin and GP-Icdo inhibit thrombin binding,implying that the low affinity receptor is indeed the previously suggested GP-I complex and does not appear to be directly involved withplatelet activation.Examination of the effect of dose and duration of incubation with non-covalently binding TLCK-T on subsequent α-thrombin response suggests the existence of positive cooperativity among thrombin receptors.Although TLCK-T has the same affinity for platelets (Kd) as T , the rateof binding and therefore that of dissociation are lower. Thus for incubation times of 1 minute or less with up to a 2x saturating TLCK-T dose, the subsequent depolarization response to a saturating T dose was enhanced. Exposure to higher TLCK-T (5x saturating)doses led to significant inhibition.Verification of the potentiation observed in noncovalent TLCK-T studies was performed using TLCK-T covalently bound to the platelet receptor with DNCO. Several hundred thrombin molecules were bound to the platelet when a subsaturating dose of TLCK-T(0.0025 U/ml) was used to crosslink, whileseveral thousand resulted with a saturating (0.05 U/ml) TLCK-T dose. Positive cooperativity was observed with low αT doses (0.005 U/ml) when several hundred high affinity receptors are blocked. The parameters studied which exhibited this positive cooperativity were depolarization, pH change and serotonin secretion, α-Glucuronidase secretion was normal. The presence and degreeof enhancement were donor-variableand suggest different threshhold thrombin dose requirements. The enhancement observed can be attributed to either an increased rate of binding (increased affinity) or to an increased number of exposed binding sites. Since little difference was found between the number of TLCK-T molecules bound after30 versus 60 seconds, we conclude that thepotentiation is more likely due to an increased number of exposed binding sites. Results from covalent crosslinks using a fluorescein and rhodamine labeled-TLCK-T and the fluorescence activated cellsorter support this hypothesis. The sensitization of the high affinity binding sitesby partial occupancy implies these bindingsites are responsible for depolarization, pH change and dense granule secretion (the rapid initial activation response), while βglucuronidase secretion, a secondary response, is otherwise controlled.
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Bowry, S. K., and M. Tepel. "NON-REVERSIBLE BINDING OF 5'-p-FLUOROSULFONYLBENZOYL ADENOSINE TO WASHED INTACT PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643506.

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ADP is an important in vivo mediator of platelet aggregation. The identification and estimation of a finite number of receptor sites has been made difficult by the reversible nature of the action of ADP on platelets and because ADP can be degraded by enzymes on the platelet surface. Analogues of ADP have therefore been commonly used to study the ADP receptor. We investigated the validity of using 5'-p-fluorosulfonylbenzoyl adenosine (FSBA), an affinity analogue of ADP that inhibits ADP-induced aggregation, for studying the ADP receptor on intact washed platelets. Binding of labelled FSBA, like for ADP, was saturable. Scatchard plot analyses of equilibrium binding data indicated, positive cooperativity; the apparent affinity (2.4 × 10−6) correlated well with the amount of ADP required to cause aggregation and with the value obtained from aggregation studies. However, the platelet bound FSBA was not displaceable with excess unlabelled FSBA indicating non-reversibility of ligand binding. As the minimal criteria for receptor identification (specificity, saturability and reversibility) are not fulfilled, the usage of FSBA to study the ADP receptor must be treated with caution. As FSBA is able to bind covalently to at least four polypeptides in isolated platelet membranes, a finite number of receptors cannot be postulated using FSBA. Furthermore, positive cooperativity, as indicated by the Scatchard plots, may be explained in terms of specific non-receptor binding. As the ADP receptor cannot be identified with any degree of certainty, the possibility therfore exists that the mechanism by which ADP initiates aggregation by rearrangement of platelet membrane proteins without binding to a single protein receptor.
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Moake, J. L., M. A. Harris, C. E. Whitley, and C. P. Alfrey. "RAPID, SENSITIVE N0N-RADI0ACTIVE QUANTIFICATION AND ANALYSIS OF PLASMA VON WILLEBRAND FACTOR (vWF) MULTIMERS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644085.

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Assessment of plasma vWF abnormalities by clinical coagulation laboratories is difficult because the available test systems for vWF antigen quantification and multimer analysis are expensive, laborious, and require days, radioactive anti-vWF antibodies and autoradiographic methods. We have devised simple, rapid, sensitive alternative techniques for vWF quantification and multimer analysis that can be readily installed in clinical laboratories. Plasma vWF antigen quantification is by a 2 hour enzyme immunoassay that accurately detects levels as low as 0.23% of normal. Plasma vWF to be quantified is bound to polyclonal monospecific antihuman vWF attached to small glass beads, and anti-human vWF conjugated with alkaline phosphatase is added to make an insoluble "sandwich." A substrate solution consisting of phenylphosphate and 4-amino-antipurine is added, followed by potassium ferricyanide. Optical density (at 490-510 nm) of the red color that develops is directly proportional to the plasma concentration of vWF antigen. Plasma vWF multimeric analysis is by a one-day electrophoretic immunobiot procedure. Plasma vWF multimer forms are solubilized in SDS-urea-Tris-EDTA, separated by horizontal 1% agarose gel electrophoresis, and transferred to a cationic membrane. Other protein binding sites on the membrane are blocked with milk proteins, and the membrane is overlaid with anti-vWF IgG linked to alkaline phosphatase. vWF multimers are then displayed as blue bands by soaking the membrane in an alkaline solution of the histochemical stain, fast blue RR (commonly used for leukocyte alkaline phosphatase scoring) dissolved in naphtol AS-MX phosphate. These simple, non-radioactive procedures performed together permit the rapid distinction of classical (Type I) von Willebrand's disease (vWD), characterized by low vWF antigen and normal multimers, from the Type II vWD syndromes, characterized by a relative deficiency of the largest plasma vWF forms. Unusually large vWF multimers, present in remission plasma of patients with chronic relapsing thrombotic thrombocytopenic purpura (TTP), are also easily detected using this rapid system of multimer analysis.
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Reports on the topic "Membrane bound proteins"

1

Smith, H. G. Surface-Bound Membrane-Mimetic Assemblies: Electrostatic Attributes of Integral Membrane Proteins. Fort Belvoir, VA: Defense Technical Information Center, October 1988. http://dx.doi.org/10.21236/ada204381.

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2

Smith, H. G. Surface-Bound Membrane-Mimetic Assemblies: Electrostatic Attributes of Integral Membrane Proteins. Fort Belvoir, VA: Defense Technical Information Center, June 1991. http://dx.doi.org/10.21236/ada237229.

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