Relevant bibliographies by topics / Biochemistry of glycoproteins

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

Academic literature on the topic 'Biochemistry of glycoproteins'

Author: Grafiati
Published: 4 June 2021
Last updated: 11 February 2022

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Journal articles on the topic "Biochemistry of glycoproteins"

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Quinn, Derek J., Neil V. McFerran, John Nelson, and W. Paul Duprex. "Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology." Bioscience Reports 32, no. 3 (March 29, 2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.

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Protein interactions play key roles throughout all subcellular compartments. In the present paper, we report the visualization of protein interactions throughout living mammalian cells using two oligomerizing MV (measles virus) transmembrane glycoproteins, the H (haemagglutinin) and the F (fusion) glycoproteins, which mediate MV entry into permissive cells. BiFC (bimolecular fluorescence complementation) has been used to examine the dimerization of these viral glycoproteins. The H glycoprotein is a type II membrane-receptor-binding homodimeric glycoprotein and the F glycoprotein is a type I disulfide-linked membrane glycoprotein which homotrimerizes. Together they co-operate to allow the enveloped virus to enter a cell by fusing the viral and cellular membranes. We generated a pair of chimaeric H glycoproteins linked to complementary fragments of EGFP (enhanced green fluorescent protein) – haptoEGFPs – which, on association, generate fluorescence. Homodimerization of H glycoproteins specifically drives this association, leading to the generation of a fluorescent signal in the ER (endoplasmic reticulum), the Golgi and at the plasma membrane. Similarly, the generation of a pair of corresponding F glycoprotein–haptoEGFP chimaeras also produced a comparable fluorescent signal. Co-expression of H and F glycoprotein chimaeras linked to complementary haptoEGFPs led to the formation of fluorescent fusion complexes at the cell surface which retained their biological activity as evidenced by cell-to-cell fusion.
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Steven, A. C. "BIOCHEMISTRY: Viral Glycoproteins and an Evolutionary Conundrum." Science 313, no. 5784 (July 14, 2006): 177–78. http://dx.doi.org/10.1126/science.1129761.

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Garner, Omai B., and Linda G. Baum. "Galectin–glycan lattices regulate cell-surface glycoprotein organization and signalling." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1472–77. http://dx.doi.org/10.1042/bst0361472.

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The formation of multivalent complexes of soluble galectins with glycoprotein receptors on the plasma membrane helps to organize glycoprotein assemblies on the surface of the cell. In some cell types, this formation of galectin–glycan lattices or scaffolds is critical for organizing plasma membrane domains, such as lipid rafts, or for targeted delivery of glycoproteins to the apical or basolateral surface. Galectin–glycan lattice formation is also involved in regulating the signalling threshold of some cell-surface glycoproteins, including T-cell receptors and growth factor receptors. Finally, galectin–glycan lattices can determine receptor residency time by inhibiting endocytosis of glycoprotein receptors from the cell surface, thus modulating the magnitude or duration of signalling from the cell surface. This paper reviews recent evidence in vitro and in vivo for critical physiological and cellular functions that are regulated by galectin–glycoprotein interactions.
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UEDA, Kazumitsu. "Biochemistry of Human P-Glycoproteins, the Multidrug Transporter." Journal of the agricultural chemical society of Japan 66, no. 11 (1992): 1617–24. http://dx.doi.org/10.1271/nogeikagaku1924.66.1617.

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Kukushkin, Nikolay V., Dominic S. Alonzi, Raymond A. Dwek, and Terry D. Butters. "Demonstration that endoplasmic reticulum-associated degradation of glycoproteins can occur downstream of processing by endomannosidase." Biochemical Journal 438, no. 1 (July 27, 2011): 133–42. http://dx.doi.org/10.1042/bj20110186.

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During quality control in the ER (endoplasmic reticulum), nascent glycoproteins are deglucosylated by ER glucosidases I and II. In the post-ER compartments, glycoprotein endo-α-mannosidase provides an alternative route for deglucosylation. Previous evidence suggests that endomannosidase non-selectively deglucosylates glycoproteins that escape quality control in the ER, facilitating secretion of aberrantly folded as well as normal glycoproteins. In the present study, we employed FOS (free oligosaccharides) released from degrading glycoproteins as biomarkers of ERAD (ER-associated degradation), allowing us to gain a global rather than single protein-centred view of ERAD. Glucosidase inhibition was used to discriminate between glucosidase- and endomannosidase-mediated ERAD pathways. Endomannosidase expression was manipulated in CHO (Chinese-hamster ovary)-K1 cells, naturally lacking a functional version of the enzyme, and HEK (human embryonic kidney)-293T cells. Endomannosidase was shown to decrease the levels of total FOS, suggesting decreased rates of ERAD. However, following pharmacological inhibition of ER glucosidases I and II, endomannosidase expression resulted in a partial switch between glucosylated FOS, released from ER-confined glycoproteins, to deglucosylated FOS, released from endomannosidase-processed glycoproteins transported from the Golgi/ERGIC (ER/Golgi intermediate compartment) to the ER. Using this approach, we have identified a previously unknown pathway of glycoprotein flow, undetectable by the commonly employed methods, in which secretory cargo is targeted back to the ER after being processed by endomannosidase.
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Bieńkowska-Szewczyk, K., and B. Szewczyk. "Expression of genes coding for animal virus glycoproteins in heterologous systems." Acta Biochimica Polonica 46, no. 2 (June 30, 1999): 325–39. http://dx.doi.org/10.18388/abp.1999_4166.

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The outermost layers of animal viruses are usually composed of glycoproteins. They are responsible not only for the entrance of viruses into, and release from host cells but also for the initial interaction of a viral particle with immunological defense of the host. It is therefore not surprising that many laboratories devote a lot of effort to study viral glycoproteins at the molecular level. Very often such studies are possible only after the introduction of a glycoprotein gene into a heterologous system. Expression of glycoprotein genes is usually obtained in mammalian or insect cells. Expression in mammalian cells yields viral glycoproteins with glycan chains indistinguishable from the original counterparts in virion particles but the level of synthesis of glycoproteins is very low. Vaccinia virus is the most common vector for expression in mammalian cells. It is easy to grow, the introduction of foreign genes is relatively simple and, due to the size of the vaccinia genome, it can accept large pieces of foreign DNA. Glycosylation in insect cells is not as complex as in mammalian cells and usually glycoproteins produced in insect cells are of slightly lower molecular mass than those produced in mammalian cells. The most common vector for expression of glycoproteins in insect cells is a baculovirus, Autographa californica nuclear polyhedrosis virus (AcNPV). The great advantage of this system is a very high level of expression of foreign genes.
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Browning, Darren D., and Danton H. O'Day. "Concanavalin A and wheat germ agglutinin binding glycoproteins associated with cell fusion and zygote differentiation in Dictyostelium discoideum: effects of calcium ions and tunicamycin on glycoprotein profiles." Biochemistry and Cell Biology 69, no. 4 (April 1, 1991): 282–90. http://dx.doi.org/10.1139/o91-043.

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To determine which glycoproteins may be critical to sexual development in Dictyostelium discoideum, cell samples from different developmental stages were separated by sodium dodecyl sulfate – polyacrylamide gel electrophoresis and blotted to nitrocellulose. Concanavalin A (ConA) and wheat germ agglutinin (WGA) binding proteins were visualized on the blots using an immunochemical procedure employing peroxidase–antiperoxidase. ConA labelled at least 28 proteins, but only one band showed calcium-dependent changes in its expression. WGA bound at least 30 proteins and changes in several bands were observed that did not occur in calcium-deficient controls. Two WGA-binding glycoproteins which migrated at 200 and 166 kilodaltons (kDa), respectively, showed developmental changes associated with the time of cell fusion. One WGA-binding and one ConA-binding glycoprotein migrating at 130 and 126 kDa, respectively, appeared later during sexual development, in association with the phase of zygote differentiation. Several WGA- and ConA-binding glycoproteins decreased during sexual development, but were not affected by the absence of calcium ions. Tunicamycin (1 μg/mL) inhibited cell fusion when added to sexual cultures prior to the appearance of the 166-kDa glycoprotein gp166. The effects of this inhibitor on development support the importance of glycoproteins to cell fusion during sexual development in D. discoideum.Key words: Dictyostelium, cell fusion, glycoprotein, tunicamycin, concanavalin A, wheat germ agglutinin, calcium.
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Pan, Y. T., Hidetaka Hori, and Alan D. Elbein. "The effect of glycoprotein-processing inhibitors on the secretion of glycoproteins by Madin-Darby canine kidney cells." Biochemistry and Cell Biology 65, no. 4 (April 1, 1987): 345–53. http://dx.doi.org/10.1139/o87-044.

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The effects of various glycoprotein-processing inhibitors on the biosynthesis and secretion of N-linked glycoproteins was examined in cultured Madin-Darby canine kidney (MDCK) cells. Since incorporation of [2-3H]mannose into lipid-linked saccharides and into glycoproteins was much greater in phosphate-buffered saline (PBS) than in serum-supplemented basal medium (BME), most experiments were done in PBS. Castanospermine, an inhibitor of glucosidase I, caused the formation of glycoproteins having mostly Glc3Man7–9(GlcNAc)2 structures; deoxymannojirimycin, an inhibitor of mannosidase I, gave mostly glycoproteins with Man9(GlcNAc)2 structures; swainsonine, an inhibitor of mannosidase II, caused the accumulation of hybrid types of oligosaccharides. Castanospermine and swainsonine, either in PBS or in BME medium, had no effect on the incorporation of [2-3H]mannose or [5,6-3H]leucine into the secreted glycoproteins and, in fact, there was some increase in mannose incorporation in their presence. These inhibitors also did not affect mannose incorporation into cellular glycoproteins nor did they affect the biosynthesis as measured by mannose incorporation into lipid-linked saccharides. On the other hand in PBS medium, deoxymannojirimycin, at 25 μg/mL, caused a 75% inhibition in mannose incorporation into secreted glycoproteins, but had no effect on the incorporation of [3H]leucine into the secreted glycoproteins. Since deoxymannojirimycin also strongly inhibited mannose incorporation into lipid-linked oligosaccharides in PBS, the decreased amount of radioactivity in the secreted and cellular glycoproteins may reflect the formation of glycoproteins with fewer than normal numbers of oligosaccharide chains, owing to the low levels of oligosaccharide donor. However, in BME medium, there was only slight inhibition of mannose incorporation into lipid-linked saccharides and into cellular and secreted glycoproteins.
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Michelson, AD, and MR Barnard. "Thrombin-induced changes in platelet membrane glycoproteins Ib, IX, and IIb-IIIa complex." Blood 70, no. 5 (November 1, 1987): 1673–78. http://dx.doi.org/10.1182/blood.v70.5.1673.1673.

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Abstract Platelet membrane glycoprotein Ib (GPIb) and the GPIIb-IIIa complex have central roles in the interaction of platelets with the plasma coagulation system, damaged vessel walls, and other platelets. We investigated the effects of thrombin on these glycoproteins. Monoclonal antibodies were used to assess platelet surface glycoproteins by flow cytometry, total platelet glycoprotein content by immunoassay, and glycoproteins released from platelets, also by immunoassay. Five new observations were made with regard to thrombin-induced changes in platelet membrane glycoproteins: (a) The marked decrease in platelet surface binding of antibodies directed at GPIb was not confined to antibodies directed at the von Willebrand factor binding site. (b) There was a marked decrease in platelet surface binding of an antibody directed at GPIX, with maintenance of the 1:1 ratio of platelet surface binding of antibodies directed at GPIb and GPIX. (c) Changes in platelet surface binding of antibodies were not restricted to a distinct subpopulation of platelets. (d) There was no associated platelet release of glycocalicin (a proteolytic fragment of GPIb). (e) There was no associated platelet release of the GPIIb-IIIa complex. These thrombin-induced changes may be important in modulating the reactivity of platelets with the damaged vessel wall and with each other.
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Michelson, AD, and MR Barnard. "Thrombin-induced changes in platelet membrane glycoproteins Ib, IX, and IIb-IIIa complex." Blood 70, no. 5 (November 1, 1987): 1673–78. http://dx.doi.org/10.1182/blood.v70.5.1673.bloodjournal7051673.

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Platelet membrane glycoprotein Ib (GPIb) and the GPIIb-IIIa complex have central roles in the interaction of platelets with the plasma coagulation system, damaged vessel walls, and other platelets. We investigated the effects of thrombin on these glycoproteins. Monoclonal antibodies were used to assess platelet surface glycoproteins by flow cytometry, total platelet glycoprotein content by immunoassay, and glycoproteins released from platelets, also by immunoassay. Five new observations were made with regard to thrombin-induced changes in platelet membrane glycoproteins: (a) The marked decrease in platelet surface binding of antibodies directed at GPIb was not confined to antibodies directed at the von Willebrand factor binding site. (b) There was a marked decrease in platelet surface binding of an antibody directed at GPIX, with maintenance of the 1:1 ratio of platelet surface binding of antibodies directed at GPIb and GPIX. (c) Changes in platelet surface binding of antibodies were not restricted to a distinct subpopulation of platelets. (d) There was no associated platelet release of glycocalicin (a proteolytic fragment of GPIb). (e) There was no associated platelet release of the GPIIb-IIIa complex. These thrombin-induced changes may be important in modulating the reactivity of platelets with the damaged vessel wall and with each other.
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Dissertations / Theses on the topic "Biochemistry of glycoproteins"

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Jefferies, W. A. "Lymphocyte surface glycoproteins." Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355757.

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Duffy, Iain. "Analysis of measles virus glycoproteins." Thesis, Queen's University Belfast, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.324842.

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Wood, Sarah Louise. "Glycoproteins of the chromaffin granule membrane." Thesis, University of Edinburgh, 1987. http://hdl.handle.net/1842/19427.

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Howe, T. "Biosynthesis of serum glycoproteins by isolated rat hepatocytes." Thesis, Bucks New University, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.371224.

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Burdge, Graham Charles. "Biochemical analysis of proteolytic fragments from desmosomal glycoproteins." Thesis, University of Southampton, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.290426.

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Hemming, Richard John. "Radioautographical and biochemical studies on nucleoplasmic glycoproteins." Thesis, McGill University, 1992. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=41298.

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EM radioautography was used to examine the tissue distribution of cells exhibiting nucleoplasmic labeling after being exposed to $ sp3$H-sugars or $ sp{35}$S-sulphate to indicate the general extent of the occurrence of nucleoplasmic glycoproteins within animal cells. The observation of some degree of such labeling in virtually all cells in tissues of three animal species suggests that nucleoplasmic glycoproteins are a common cellular feature. To better define the distribution and nature of the putative labeled nucleoplasmic glycoproteins, cultured cells were used as a model cell type for both quantitative EM radioautographic and biochemical studies. After exposure to $ sp3$H-sugars, all three lines of cultured cells examined exhibited significant nucleoplasmic reaction in which the euchromatin, heterochromatin and nucleoli were all labeled to some extent. Studies on isolated, envelope-depleted nuclei from myeloma cells confirmed that the molecules in the nucleoplasm itself were the source of the radioautographic reaction observed over nuclei. Biochemical analyses of fractions of isolated nuclei indicated that much of the label resided in nuclear matrix glycoproteins of different molecular weights. Lectin binding studies on nuclear matrix fractions revealed the presence of galactose, fucose, and/or sialic acid residues in proteins. Glycosidase experiments indicated that some but not all of these glycoproteins had N-linked sidechains.
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Smith, Kevin David. "The site-specific glycosylation patterns of serum and membrane glycoproteins." Thesis, University of Cambridge, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315282.

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Brown, Vivienne Alison. "A study of cell surface glycoproteins in chronic lymphocytic leukaemia." Thesis, University of Edinburgh, 1987. http://hdl.handle.net/1842/12092.

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Zamani, Mohammad Reza. "The role of glycoproteins in neural plasticity in domestic chick." Thesis, Open University, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293893.

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Uysal, Hamdi. "Extracellular matrix glycoproteins of skin fibroblasts in tuberous sclerosis." Thesis, University of Nottingham, 1995. http://eprints.nottingham.ac.uk/13094/.

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The first main objective of this project was to isolate cellular fibronectin from cultures of skin fibroblasts derived from tuberous sclerosis (TS) patients and normals and to compare their structures, paying particular attention to the content and pattern of carbohydrate (glycosylation). The second main objective of this project was to establish the expression and localisation of glycoproteins fibronectin, laminin and tenascin of the extracellular matrix (ECM) in cultures of skin fibroblasts derived from patients with TS and normal individuals. In order to achieve these objectives, fibroblasts were established from primary cultures of skin explants of patients with TS. Control cells were cultured from skin explants donated by people not known to be suffering from any disorder. The purification of cellular fibronectin was achieved from conditioned medium of skin fibroblasts of TS patients and control fibroblasts using Prosep-gelatin affinity chromatography and gel filtration chromatography techniques. Analysis of purified cellular fibronectin by high pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD) revealed that the carbohydrate portion of the fibronectin molecule was made up of galactose, mannose, glucosamine, galactosamine, sialic acid and fucose. An increased concentration of sialic acid, galactosamine, glucosamine, galactose and mannose was observed in purified fibronectin derived from neck and ungual fibromas of patients with TS. To provide a total increase of carbohydrates more than two fold in comparison to normal fibroblastsderived fibronectin. Purified cellular fibronectin from conditioned medium of fibroblasts grown from skin lesions of different TS patients and from normal skin fibroblasts did not express HNK-1 (anti-leu 7) carbohydrate epitope. Normal skin fibroblasts showed an altered morphology and less confluence when grown on cell culture plates coated with cellular fibronectin derived from TS fibroblasts compared with control fibronectin. This may be a consequence of an altered glycosylation of this protein. The amino acid composition of the purified fibronectin from TS fibroblasts was very similar to that purified fibronectins from normal fibroblasts and to standard commercial plasma and cellular fibronectins. Laminin and tenascin were partially purified from conditioned cell culture medium demonstrating their synthesis and secretion into the cell culture medium by dermal skin fibroblasts. Expression and distribution of fibronectin, tenascin and laminin by established TS and normal skin fibroblasts using immunofluorescence, ELISA, and flow cytometry techniques were analysed and presented qualitative and quantitatively in this thesis. Increased expression and altered distribution of fibronectin and tenascin were observed in the fibroblasts derived from ungual fibroma lesion of a TS patient, but not in fibroblasts of neck fibroma, forehead plaque lesion or unaffacted skin of TS patients in comparison to control fibroblasts. However, increased expression and altered distribution of laminin were observed in neck fibroma-derived fibroblasts in contrast to fibronectin and tenascin. Laminin expression was not changed in ungual fibroma and forehead plaque lesion-derived fibroblasts in comparison to control fibroblasts. Altered distribution of fibronectin was well observed by immunofluorescence particularly in large cells of ungual fibroma. Similar differences were observed with laminin of cells from neck fibroma of TS patients. These results suggest the abnormal assembly of ECM in different TS skin lesions. Abnormal migration of cells during early embryonic development and the hardening of tissues associated with TS may result from abnormal assembly of the ECM. Alterations in distribution and structure of these adhesive glycoproteins may cause functional disruption in their binding and interactions with cells and ECM macromolecules. Studies of these changes in the ECM components may contribute to the understanding of the mechanisms involved in the aetiology of hardened tissues of TS.
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Books on the topic "Biochemistry of glycoproteins"

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Owens, Raymond. Functional and Structural Proteomics of Glycoproteins. Dordrecht: Springer Science+Business Media B.V., 2011.

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European Symposium on Carbohydrates (3rd 1985 Grenoble, France). Euro-carbohydrates 1985: Abstracts of the Third European Symposium on Carbohydrates : chemistry, biochemistry, technology : Grenoble, France, September 16-20, 1985 = Troisième Symposium européen sur les glucides : chimie, biochimie, technologie : resumés. Grenoble: Impr. de la Bibliothèque interuniversitaire, 1985.

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Kühl, Michael. Wnt signaling in development. Georgetown, Tex: Landes Bioscience, 2003.

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(Editor), J. Montreuil, J.F.G. Vliegenthart (Editor), and H. Schachter (Editor), eds. Glycoproteins I (New Comprehensive Biochemistry). Elsevier Science, 1995.

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(Editor), J. Montreuil, J.F.G. Vliegenthart (Editor), and H. Schachter (Editor), eds. Glycoproteins I (New Comprehensive Biochemistry). Elsevier Science, 1995.

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Lennarz, William. The Biochemistry of Glycoproteins and Proteoglycans. Springer, 2012.

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The Biochemistry of Glycoproteins and Proteoglycans. Springer, 2012.

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H, Greiling. Keratan Sulphate Proteoglycans Chemistry, Biochemistry, Biology and Chemical Pathology. Ashgate Publishing, 1989.

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Euro-carbohydrates 1985: Abstracts of the Third European Symposium on Carbohydrates : chemistry, biochemistry, technology : Grenoble, France, September ... : chimie, biochimie, technologie : Resumes. Impr. de la Bibliotheque interuniversitaire, 1985.

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1944-, Brauman P., ed. Alpha1-acid glycoprotein: Genetics, biochemistry, physiological functions, and pharmacology : proceedings of a meeting held in Prilly-Lausanne, Switzerland, September 1-2, 1988. New York: Liss, 1989.

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Book chapters on the topic "Biochemistry of glycoproteins"

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Mattos, Eliciane C., Renata R. Tonelli, Walter Colli, and Maria Julia M. Alves. "The Gp85 Surface Glycoproteins from Trypanosoma cruzi." In Subcellular Biochemistry, 151–80. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-7305-9_7.

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Rimmer, Eric F., and Michael A. Horton. "Membrane Glycoproteins of Mast Cells and Basophils." In Blood Cell Biochemistry, 369–407. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3796-0_13.

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Duperray, Alain, Rolande Berthier, and Gérard Marguerie. "Biosynthesis and Processing of Platelet Glycoproteins in Megakaryocytes." In Blood Cell Biochemistry, 37–58. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9531-8_2.

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Green, F. R., P. Greenwell, L. Dickson, B. Griffiths, J. Noades, D. M. Swallow, and P. Greenwell. "Expression of the ABH, Lewis, and Related Antigens on the Glycoproteins of the Human Jejunal Brush Border." In Subcellular Biochemistry, 119–53. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-1681-5_4.

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Herp, Anthony, Carol Borelli, and Albert M. Wu. "Biochemistry and Lectin Binding Properties of Mammalian Salivary Mucous Glycoproteins." In The Molecular Immunology of Complex Carbohydrates, 395–435. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1663-3_15.

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Damsky, C. H., K. A. Knudsen, A. F. Horwitz, M. J. Wheelock, P. Gruber, and C. A. Buck. "Integral Membrane Adhesion Glycoproteins: What is their Fate During Metastasis?" In Biochemistry and Molecular Genetics of Cancer Metastasis, 25–42. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2299-3_3.

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Gould-Fogerite, Susan, Joseph E. Mazurkiewicz, Donna Bhisitkul, and Raphael J. Mannino. "The Reconstitution of Biologically Active Glycoproteins into Large Liposomes: Use as a Delivery Vehicle to Animal Cells." In Advances in Membrane Biochemistry and Bioenergetics, 569–86. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4684-8640-7_56.

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Kim, Cheorl-Ho. "Congenital Disorders of Glycosylation (CDG) of N-Glycoprotein." In Ganglioside Biochemistry, 55–58. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-5815-3_4.

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Springeii, Timothy A., and Donald C. Anderson. "The Importance of the Mac-1, LFA-1 Glycoprotein Family in Monocyte and Granulocyte Adherence, Chemotaxis, and Migration into Inflammatory Sites: Insights from an Experiment of Nature." In Ciba Foundation Symposium 118 - Biochemistry of Macrophages, 102–26. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720998.ch8.

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Metzler, David E., Carol M. Metzler, and David J. Sauke. "Sugars, Polysaccharides, and Glycoproteins." In Biochemistry, 161–97. Elsevier, 2001. http://dx.doi.org/10.1016/b978-012492543-4/50007-6.

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Conference papers on the topic "Biochemistry of glycoproteins"

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Harmon, J. T., and G. A. Jamieson. "TWO SIZES OF THROMBIN RECEPTORS IN SOLUBILIZED HUMAN PLATELET MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644468.

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Thrombin receptors of two functional sizes (106 and 30,000) have been previously identified by the technique of radiation inactivation (Harmon and Jamieson, Biochemistry 24:58, 1985). To determine whether different s-ized populations are separable biochemically, platelet membranes solubilized in Triton X-100 were applied to a Sepharose 6B column after incubation with 125I-thrombin. Apart from unbound 125I-thrombin (40,000) the elution profile showed two radioactive peaks with apparent mol. wts. of 1−2×106 and 170,000. The bound radioactivity associated with these two peaks could be competed by nonradioactive thrombin. Chromatography was then carried out in the absence of added thrombin and the specific thrombin binding activity of the eluted fractions was determined by a soluble radioreceptor assay (Harmon and Jamieson, J. Biol. Chem. 261:13224, 1986): two peaks with apparent mol. wts. of 1−2×106 and 170,000 were again observed. Western blotting with polyclonal rabbit anti-glycocalicin antibody showed that intact glycoprotein lb (GPIb) was associated with the high mol. wt. peak while a fragment of GPIb (Mr 120,000) was associated with the lower mol. wt. peak. Thus, in solubilized platelet membranes, thrombin binding activity exists in two mol. wt. forms (1−2×106 and 170,000) and both are associated with GPIb-like molecules. Other membrane components associated with these complexes remain to be determined.
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Koedam, Joost A., Rob J. Hamer, Nel H. Beeser-Visser, Etienne Jap Tjoen San, Kees Schippers, and Jan J. Sixma. "THE INTERACTION BETWEEN FACTOR VIII AND VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644771.

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Factor VIII (FVIII) circulates in plasma as a non-covalent complex with von Willebrand factor (VWF), a large multimeric adhesive glycoprotein. VWF serves as a carrier for FVIII and is thought to stabilize FVIII. The interaction between the two proteins was studied by binding purified human 125I-FVIII to VWF which was coated on a solid matrix. Experiments employing isolated heavy and light chains of FVIII and monoclonal antibodies indicated that binding occurred through the carboxyterminal 80kDa light chain of factor VIII. Treatment of VWF-bound 125I-FVIII with thrombin resulted in the release of a light chain-derived 70kDa fragment and a heavy chain-derived 50kDa fragment. A 42kDa heavy chain-derived fragment was found in the fraction which remained bound to VWF. Treatment with factor Xa (FXa) resulted in the release of 63, 50, 45, and 42kDa fragments. No phospholipids were required for proteolysis of FVIII by either of these enzymes. In solution, the activation of FVIII by FXa, but not by thrombin, was inhibited by VWF. Neither activation, nor cleavage or release from VWF were observed when FVIII was incubated with factor IXa. Activation of FVIII was parallelled by its release from VWF. We conclude that the thrombin-activated form of FVIII consists of a complex between the 70kDa and 50kDa fragments. Inactivation of FVIII by activated protein C (APC) was inhibited when FVIII was complexed to VWF. This protective effect of VWF was abolished upon activation of FVIII and its subsequent release from VWF.In order to locate the binding site for FVIII on the VWF molecule, we digested VWF with Staphylococcal V8 protease (Sp). Digestion products were isolated with Mono Q ion-exchange chromatography and identified as Spl (39 kDa), SpII dimers (220 kDa) and Spill dimers (a triplet ranging from 210-280 kDa) by their molecular weight and chromatographic behaviour (J.-P. Girma et al.. Biochemistry 1986, 25:3156-3163). Purified VWF or digestion products were spotted on nitrocellulose paper, followed by blocking with an albumin solution. Binding of FVIII was studied by incubating the filters with 125I-FVIII, followed by autoradiography. Fifty ng of VWF was sufficient in order to detect FVIII binding. No binding was observed to partially reduced dimeric undigested VWF. Of the isolated digestion products, only the SpIII dimer was able to bind 125I-FVIII. After Western blotting of VWF-fragments from SDS-polyacrylamide gels, 125I-FVIII bound only to the bands which represented SpIII. Therefore, the domain on VWF responsible for the binding of FVIII seems to be located on its aminoterminal SpIII fragment. The integrity of internal disulfide bonds and dimerisation of VWF are required for FVIII binding.
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