Relevant bibliographies by topics / Guanidinium chloride

Contents

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

Academic literature on the topic 'Guanidinium chloride'

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

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Guanidinium chloride.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Guanidinium chloride"

1

Mazzini, Alberto, and Roberto Favilla. "The Effect of Guanidinium Chloride on the Self-Association of Bovine Liver Glutamate Dehydrogenase: A Gel Filtration Study." Zeitschrift für Naturforschung C 42, no. 3 (March 1, 1987): 217–20. http://dx.doi.org/10.1515/znc-1987-0308.

Full text
Abstract:
The associative behaviour of bovine liver glutamate dehydrogenase has been studied by gel chromatography at neutral pH in 1 ᴍ guanidinium chloride and 1 ᴍ sodium chloride. In guanidinium chloride both the elution volume and the elution profile of the enzyme are independ­ent of protein concentration, whereas in sodium chloride they are strongly dependent on it. In NaCl the enzyme behaves as expected according to the well established random association model, whereas in guanidinium chloride it appears to have completely lost the self-associative property. Furthermore, since the elution volume of the enzyme in guanidinium chloride corre­sponds to that of an hexamer, trimer formation reported to occur in these conditions is not confirmed by this technique.
APA, Harvard, Vancouver, ISO, and other styles
2

Kantlehner, Willi, Jochen Mezger, Ralf Kreß, Horst Hartmann, Thorsten Moschny, Ioannis Tiritiris, Boyan Iliev, et al. "Orthoamide, LXIX [1]. Beiträge zur Synthese N,N,N´,N´,N´´-peralkylierter Guanidine und N,N,N´,N´,N´´䞲,N´´-persubstituierter Guanidiniumsalze / Orthoamides, LXIX [1]. Contributions to the Synthesis of N, N, N´, N´, N´-peralkylated Guanidines and N, N, N´, N´, N´´, N´´-persubstituted Guanidinium Salts." Zeitschrift für Naturforschung B 65, no. 7 (July 1, 2010): 873–906. http://dx.doi.org/10.1515/znb-2010-0712.

Full text
Abstract:
N, N, N´, N´-Tetraalkyl-chloroformamidinium chlorides 6 are prepared from N, N, N´, N´-tetraalkylureas 5 and phosgene in acetonitrile. The iminium salts 6 react with primary and secondary amines in the presence of triethylamine to give N, N, N´, N´, N´´-pentasubstituted and N, N, N´, N´, N´´, N´´- hexasubstituted guanidinium salts 7 and 8, respectively, Treatment of the guanidinium salts 7 with sodium hydroxide in excess affords the N, N, N´N´, N´´-pentasubstituted guanidines 9a - 9aa. Additionally, the N, N, N´, N´, N´´-pentasubstituted and N, N, N´, N´, N´´, N´´-hexasubstituted guanidinium salts 7l´, 7p´ and 8a - c can be obtained from the reaction mixtures by addition of stoichiometric amounts of sodium hydroxide. A modified method is described for the preparation of guanidinium salts possessing dialkylamino substituents consisting of two long-chain alkyl groups (>C14). Some guanidines 9 were alkylated with allyl chloride and bromide, ethyl bromide, butyl bromide, benzyl bromide and chloride, dimethyl sulfate, diethyl sulfate, and methyl methansulfonate to give the corresponding guanidinium salts 11 - 15. By alkylation of the N, N, N´, N´, N´´-pentasubstituted guanidine 9v with triethyloxonium tetrafluoroborate the guandinium tetrafluoroborate 16a is accessible. N-Functionalized guanidinium salts 17 - 18a - c result from the reaction of N, N, N´, N´, N´´-pentasubstituted guanidines with ethyl bromoacetate and bromoacetonitrile, respectively, and subsequent anion exchange with sodium tetraphenylborate. N, N, N´, N´-Tetramethylguanidine (21) adds to ethyl acrylate to give the labile guanidine 22, which forms the guanidinium salt 23a on treatment with methyl iodide. Zwitterionic guanidinium salts 25 result, when N, N, N´, N´, N´´-pentasubstituted guanidines are treated with sultones 24.
APA, Harvard, Vancouver, ISO, and other styles
3

Puri, N. K., E. Crivelli, M. Cardamone, R. Fiddes, J. Bertolini, B. Ninham, and M. R. Brandon. "Solubilization of growth hormone and other recombinant proteins from Escherichia coli inclusion bodies by using a cationic surfactant." Biochemical Journal 285, no. 3 (August 1, 1992): 871–79. http://dx.doi.org/10.1042/bj2850871.

Full text
Abstract:
Recombinant pig growth hormone (rPGH) was solubilized from inclusion bodies by using the cationic surfactant cetyltrimethylammonium chloride (CTAC). The solubilizing action of CTAC appeared to be dependent on the presence of a positively charged head group, as a non-charged variant was inactive. Relatively low concentrations of CTAC were required for rapid solubilization, and protein-bound CTAC was easily removed by ion-exchange chromatography. Compared with solubilization and recovery of rPGH from inclusion bodies with 7.5 M-urea and 6 M-guanidinium chloride, the relative efficiency of solubilization was lower with CTAC. However, superior refolding efficiency resulted in final yields of purified rPGH being in the order of CTAC greater than urea greater than or equal to guanidinium chloride. Detailed comparison of the different rPGH preparations as well as pituitary-derived growth hormone by h.p.l.c., native PAGE, c.d. spectral analysis and radioreceptor-binding assay showed that the CTAC-derived rPGH was essentially indistinguishable from the urea and guanidinium chloride preparations. The CTAC-derived rPGH was of greater biopotency than pituitary-derived growth hormone. The advantages of CTAC over urea and guanidinium chloride for increasing recovery of monomeric rPGH by minimizing aggregation during refolding in vitro were also found with recombinant sheep interleukin-I beta and a sheep insulin-like growth factor II fusion protein. In addition, the bioactivity of the CTAC-derived recombinant interleukin-1 beta was approximately ten-fold greater than that of an equivalent amount obtained from urea and guanidinium chloride preparations. It is concluded that CTAC represents, in general, an excellent additional approach or a superior alternative to urea and in particular guanidinium chloride for solubilization and recovery of bioactive recombinant proteins from inclusion bodies.
APA, Harvard, Vancouver, ISO, and other styles
4

Goward, C. R., L. I. Irons, J. P. Murphy, and T. Atkinson. "The secondary structure of protein G′, a robust molecule." Biochemical Journal 274, no. 2 (March 1, 1991): 503–7. http://dx.doi.org/10.1042/bj2740503.

Full text
Abstract:
The secondary structure of recombinant streptococcal Protein G' was predicted and compared with spectropolarimetric data. The predicted secondary structure consisted of 37 +/- 4% alpha-helix and 30 +/- 5% beta-sheet, whereas the values obtained from c.d. data were 29 +/- 2% alpha-helix and 41 +/- 3% beta-sheet. An alpha-helix-beta-sheet/turn-alpha-helix motif is conjectured to comprise the Fc-binding unit. The c.d. spectra in the near u.v. and far u.v. show that the Protein G' molecule is stable to heating at 100 degrees C and to extremes of pH (pH 1.5 to 11.0). The protein retained biological activity at these extremes. The molecule uncoils above pH 11.5 in a time-dependent fashion. Unfolding of the molecule in guanidinium chloride was monitored by c.d. and fluorescence emission; 3 M-guanidinium chloride was required to unfold the protein by 50%. The protein was completely unfolded in 5.5 M-guanidinium chloride and fully refolded with restoration of activity after removal of guanidinium chloride.
APA, Harvard, Vancouver, ISO, and other styles
5

Kantlehner, Willi, Ralf Kreß, Jochen Mezger, and Georg Ziegler. "Orthoamide und Iminiumsalze, LXXXVIII. Synthese N,N,N′,N′,N″,N″-persubstituierter Guanidiniumsalze aus N,N′-persubstituierten Harnstoff/Säurechlorid-Addukten**." Zeitschrift für Naturforschung B 70, no. 1 (January 1, 2015): 9–27. http://dx.doi.org/10.1515/znb-2014-0102.

Full text
Abstract:
AbstractN,N,N′,N′,N″,N″-Hexamethylguanidinium chloride9cwas prepared by treating the reaction mixture formed fromN,N,N′,N′-tetramethylurea (1a) and phthaloyl chloride (16) with dimethyltrimethylsilylamine15.N,N,N′,N′-Tetramethyl-chloroformamidinium chloride (2a) is an intermediate in this synthesis. The chloroformamidinium chloride2acan also be prepared by treating the urea1awith thionyl chloride or phosphorus pentachloride, respectively. The guanidinium salt9ccan be obtained from the crude2athus prepared and the silylamine15. From urea/phosphoryl chloride adducts and primary aromatic amines have been prepared guanidines38, which are converted toN,N′-diaryl-N,N′,N″,N″-tetramethyl-guanidinium iodides39on treatment with methyl iodide. TheN,N′,N″-trimethyl-N,N′,N″-triphenylguanidinium salt44awas prepared from the chloroformamidinium salt43andN-methylaniline. The guanidinium salt9cis the reaction product when the urea1a/POCl3adduct is treated with the silylamine15.
APA, Harvard, Vancouver, ISO, and other styles
6

Ring, Joshua R., Sean Parkin, and Peter A. Crooks. "(4-Methoxy-3-nitrobenzylideneamino)guanidinium chloride." Acta Crystallographica Section C Crystal Structure Communications 63, no. 7 (June 14, 2007): o392—o394. http://dx.doi.org/10.1107/s0108270107023475.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Wang, Bei, Pei-Zhi Zhang, Xin Chen, Ai-Quan Jia, and Qian-Feng Zhang. "Syntheses and crystal structures of guanidine hydrochlorides with two Schiff base functions as efficient colorimetric and selective sensors for fluoride." Zeitschrift für Naturforschung B 73, no. 8 (August 28, 2018): 601–9. http://dx.doi.org/10.1515/znb-2018-0102.

Full text
Abstract:
AbstractA series of guanidinium chloride derivatives have been synthesized by condensation of 1,3-diaminoguanidine monohydrochloride with heteroaromatic formaldehydes in good yields. All compounds were characterized by nuclear magnetic resonances and infrared spectroscopies, and the molecular structures of four compounds were determined by single crystal X-ray diffraction. The optical properties of these guanidinium chloride derivatives with fluoride anions were investigated, showing selective color changes from colorless to yellow or orange, red-shifted in the ultraviolet/visible absorption spectra.
APA, Harvard, Vancouver, ISO, and other styles
8

Mayr, Lorenz M., and Franz X. Schmid. "Stabilization of a protein by guanidinium chloride." Biochemistry 32, no. 31 (August 1993): 7994–98. http://dx.doi.org/10.1021/bi00082a021.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Serra, M. A., and R. B. Honzatko. "Structure of 1-(p-nitrobenzylidineamino)guanidinium chloride." Acta Crystallographica Section C Crystal Structure Communications 42, no. 12 (December 15, 1986): 1755–57. http://dx.doi.org/10.1107/s0108270186090686.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Mohamed, Shaaban K., Peter N. Horton, Mahmoud A. A. El-Remaily, and Seik Weng Ng. "2-(1,3-Benzothiazol-2-yl)guanidinium chloride." Acta Crystallographica Section E Structure Reports Online 67, no. 11 (October 29, 2011): o3132. http://dx.doi.org/10.1107/s1600536811044643.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Guanidinium chloride"

1

Lu, Hui. "Studies of protein folding and unfolding using NMR and optical methods." Thesis, University of Oxford, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337421.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Macdonald, Ryan. "The Effects of Trimethylamine-N-Oxide and Guanidinium Chloride on Aqueous Hydrophobic Contact-Pair Interactions." Elsevier - Biophysical Chemistry, 2013. http://hdl.handle.net/1993/30162.

Full text
Abstract:
Trimethylamine-N-oxide (TMAO) and guanidinium chloride (GdmCl) are both highly studied molecules in the field of protein folding/unfolding. Thermodynamic studies have shown that TMAO, an organic osmolyte, is a strong stabilizer of the protein folded state, while GdmCl is known to be one of the most effective protein denaturants. Although TMAO and GdmCl are well studied the mechanism by which they stabilize and denature proteins, respectively, is not well understood. In fact there are few studies looking at their effects on hydrophobic interactions. In this work we determine the effect of TMAO and GdmCl on hydrophobic interactions, by looking at the model system of phenyl and alkyl hydrophobic contact pairs. Contact pair formation is monitored through the use of fluorescence spectroscopy, i.e., measuring the intrinsic phenol fluorescence being quenched by carboxylate ions. Hydrophobic interactions are isolated from other interactions through a developed methodology. The results show that TMAO addition to the aqueous solvent destabilizes hydrophobic contact-pairs formed between phenol and carboxylate ions. The TMAO acts as a “denaturant” for hydrophobic interactions. For GdmCl the data shows that for small alkyl groups, acetate and propionate, hydrophobic contact-pairs are slightly stabilized or are not affected, respectively. For the larger alkyl groups GdmCl disrupts contact pair formation and destabilizes them. GdmCl’s effect on hydrophobic interactions shows a size dependence on carboxylate ion size, i.e., as carboxylate ion tail length increases the contact pair formed with phenol is destabilized to a greater degree.
APA, Harvard, Vancouver, ISO, and other styles
3

Waldmann, Lars. "Effect of L-arginine and guanidinium chloride (GdmCl) on the unfolding and refolding of hen egg-white lysozyme (HEWL)." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=975602772.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Delk, Roger Dale. "The effects of guanidinium chloride, urea and sodium dodecyl sulfate on the endoproteinase Glu-C- catalyzed hydrolysis of N-t-BOC-L-glutamic acid-gas-phenyl ester." Virtual Press, 1994. http://liblink.bsu.edu/uhtbin/catkey/897494.

Full text
Abstract:
Endoproteinase Glu-C (EPGIu-C, EC 3.4.21.19), an enzyme isolated from the bacteria Staphylococcus aureus, has been found to cleave specifically at the carboxyl-terminal side of glutamyl and aspartyl peptide bonds. EPGIu-C has been reported to be stable and active in the presence of common denaturants such as guanidinium chloride, urea and sodium dodecyl sulfate (Drapeau, G.R. (1977) Methods in Enzymology, 47:189-191). In order assess the denaturant stability and activity of EPGIu-C, the effect of three common protein denaturants, guanidinium chloride, urea, and sodium dodecyl sulfate (SDS) on the proteolytic activity of EPGIu-C was studied.The kinetics of the hydrolyis reaction catalyzed by EPGIu-C was determined using the chromophoric substrate N-tBOC-L-glutamic acid-a-phenyl ester (BGPE).To compare theurea is significantly greater at the higher concentrations of urea. These results suggest that a complete cleavage of proteins substrate by EPGlu-C might occur more rapidly in 8.0 M urea than in 6.0 M GuCl, since EPGlu-C will be operating at a significantly higher catalytic efficiency in the urea solution.
Department of Chemistry
APA, Harvard, Vancouver, ISO, and other styles
5

Aschi, Adel. "Effets du chlorure de guanidinium sur la structure et les propriétés de la caséine- beta en solution et à l'interface avec l'air." Phd thesis, Institut national agronomique paris-grignon - INA P-G, 2001. http://tel.archives-ouvertes.fr/tel-00003548.

Full text
Abstract:
Dans un solvant aqueux, la caséine beta est composée des monomères hydrophiles et hydrophobes et forme des structures micellaires sphériques, dont à partir nous pourrions extraire les caractéristiques principales, exemples la taille et les interactions entre agrégats. Les expériences précédentes ont montré qu'en présence dans la solution d'un agent dénaturant, comme le chlorure de guanidinium (GdmCl), la caséine beta passe d'un état micellaire vers un état de monomère. En présence de 3 et 4M de GdmCl, nous avons remarqué une légère différence entre les valeurs de c/I(0,c) cela traduit par le fait que les solutions de caséine beta ne présentent pas le même contraste. Donc lorsque la concentration du GdmCl augmente le contraste augmente et vise versa. La mesure du second coefficient du viriel nous a permis d'estimer les interactions intermoléculaires lorsque la protéine est dénaturée par une forte concentration de GdmCl. A fortes concentrations de GdmCl les interactions sont répulsives et que les effets de concentrations ne peuvent pas être négligés. Or nous avons remarqué encore que le second coefficients de viriel est très faible et la valeur obtenue ne prouve pas l'aspect d'un état d'une protéine dépliée, mais peut être c'est un état intermédiaire entre un régime où la caséine beta est considérée comme une chaîne gaussiènne et un autre régime où elle est considérée comme une chaîne à volume exclu. La détermination du préfacteur P et de l'exposant alpha permet encore de connaître la nature des interactions. Les valeurs obtenues montrent que la caséine beta en présence de 3M de chlorure de guanidinium se comporte comme un polymère à volume exclu. Donc à partir de ce résultat on peut confirmer l'existence des répulsions à longue distance à l'intérieure de la chaîne polypeptide, interdisent le contact entre les segments d'acides aminés. Nous avons remarqué une contradiction en comparant ce dernier résultat à celui obtenu par l'étude de A2. En fait dans la seconde étude la gamme des q, (3 < qRg < 2 Rg/b) est faible et on ne peut pas confirmer l'état de la protéine si elle est considérée comme une chaîne guaussienne ou à volume exclu. 116 La détermination de L et b met en évidence l'existence de structures résiduelles le long de la chaîne dénaturée. Mais le problème qui se pose, c'est que le modèle de Pedersen et. al n'est pas bien applicable pour la faible zone de q (qb < 3.1). L'effet de concentrations joue un rôle très important. La caséine beta en présence d'une forte concentration de chlorure de guanidinium a un rayon de giration guaussien presque égale au rayon de giration à concentration nulle. Ce résultat prouve que la protéine n'est pas dans état totalement déplié et confirme nos résultats obtenus par l'étude du second coefficient de viriel. 4M de chlorure de guanidinium ne change pas la qualité du solvant. Mais, désormais augmente de façon significative la CMC. Toujours, cette étude prouve que la physique des polymères et l'étude des protéines sont deux aspects complémentaires. Nous avons vu par une approche plutôt simple, une description de la structure des agrégats d'une protéine spécifique. Le modèle de copolymère a pu décrire la caséine beta. Les études expérimentales de la caséine beta, proche d'une interface air / liquide, qui seront présentées plus loin, indiquent également des similitudes avec l'approche théorique..87 L'effet du GdmCl sur l'adsorption de la caséine beta a été étudié par des mesures de la structure et des propriétés de surface des couches formées à l'interface air/tampon. Les mesures de réflectivité des neutrons ont montré que la quantité de protéine adsorbée diminue quand la concentration en GdmCl augmente. Ceci était prévisible du fait que le GdmCl est un agent qui dénature et augmente la solubilité des protéines. Une élévation de la température augmente la concentration de surface totale de la protéine. L'effet hydrophobe semble donc impliqué dans l'énergie d'adsorption. Aux concentrations volumiques élevées de la solution protéique, l'interprétation des résultats laisse à penser qu'une partie de la protéine adsorbée se trouve dans l'air. Ce phénomène a déjà été observé à partir de résultats obtenus par réflectivité des rayons X dans le cas de la caséine beta et par réflectivité des neutrons dans le cas de copolymères multiblocs synthétiques. Il semble donc que l'existence d'une partie de la molécule dans l'air devrait être prise en considération dans tout modèle d'adsorption de copolymères multiblocs à l'interface gaz/liquide. Les propriétés de surface des couches d'adsorption de caséine ont été interprétées à partir du modèle thermodynamique d'un polymère multibloc asymétrique..87 Ainsi, l'effet de la concentration en GdmCl est de changer la conformation des blocs bidimentionnels à partir 117 d'une structure à deux dimensions modérément écroulée vers une structure de chaîne 2 D à volume exclu. Ce changement de structure correspond à la rupture de liaisons non covalentes entre les monomères des blocs bidimentionnels, comme on peut l'attendre des propriétés du GdmCl. Une augmentation de la température semble rompre également des liaisons non covalentes et mène à un gonflement des molécules adsorbées. Ainsi, la conformation des molécules adsorbées dépend fortement d'interactions non covalentes qui ne semblent pas uniquement de nature hydrophobe. Finalement, on peut conclure que de nombreuses liaisons non covalentes contribuent à la structure des blocs solvophobes de la caséine-beta lorsque cette protéine est adsorbée à l'interface tampon/air à partir d'un milieu non dénaturant. La présence d'un concentration suffisante de dénaturant semble rompre ces intéractions et induire des comportements de polymère à volume exclu.
APA, Harvard, Vancouver, ISO, and other styles
6

Hervé, Mireille. "Étude conformationnelle de l'alpha-antiprotéase et de son complexe avec l'élastase pancréatique." Paris 11, 1988. http://www.theses.fr/1988PA112123.

Full text
Abstract:
Les transitions de dénaturation-renaturation l'équilibre, induites par le chlorure de guanidinium de l’α1 antiprotéase humaine active ou protéolysée, de l'élastase pancréatique porcine et de leur complexe covalent ont été étudiées par trois méthodes spectroscopiques: émission de fluorescence, spectrophotométrie de différence d'absorption dans l'ultra-violet et dichroïsme circulaire. La réversibilité de la dénaturation a également été étudiée par mesure du pouvoir inhibiteur de l’α1, antiprotéase ou par le retour des propriétés antigéniques. Des formes intermédiaires correspondant à des modifications conformationnelles intervenant dans la région contenant les résidus de tryptophane ont été mis en évidence avec l’α1, antiprotéase active ou protéolysée. De plus, la forme protéolysée de l'inhibiteur est stabilisée vis-à-vis du dénaturant par rapport à forme active. Dans le complexe, le comportement de l’α1 antiprotéase est comparable à celui de la forme protéolysée et la stabilité conformationnelle de l’élastase semble diminuée par rapport à celle de la proteine libre.
APA, Harvard, Vancouver, ISO, and other styles
7

Waldmann, Lars [Verfasser]. "Effect of L-arginine and guanidinium chloride (GdmCl) on the unfolding and refolding of hen egg-white lysozyme (HEWL) / von Lars Waldmann." 2005. http://d-nb.info/975602772/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Guanidinium chloride"

1

Tiefenbach, K. J., H. Durchschlag, and R. Jaenicke. "Hydrodynamic and spectroscopic analysis of the denaturation of serum albumin induced by guanidinium chloride and sodium dodecyl sulfate." In Analytical Ultracentrifugation VII, 136–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/b98023.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Byler, D. M., D. L. Lee, and C. S. Randall. "Thermal Denaturation of Elastase in the Presence and Absence of Guanidinium Chloride: An IR Spectroscopic and DSC Investigation." In ACS Symposium Series, 145–58. Washington, DC: American Chemical Society, 1999. http://dx.doi.org/10.1021/bk-2000-0750.ch007.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

"Guanidinium Chloride." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 829. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_7209.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

"RNA Isolation Protocol from Cells and Tissues." In Protocols used in Molecular Biology, edited by Pallavi Singh, 7–14. BENTHAM SCIENCE PUBLISHERS, 2020. http://dx.doi.org/10.2174/9789811439315120010005.

Full text
Abstract:
The preparation of intact ribonucleic acid is difficult because of the action of nucleases, which are liberated upon tissue homogenisation. In many cells, high concentrations of the ribonucleases are reserved in the secretory granules and upon disruption of the cell, they get mixed with the RNA and lead to its degradation. Guanidinium chloride and thiocyanate are potent chaotropic agents that reduce hydrophobic interactions and disrupt protein tertiary structures, disassociate proteinnucleic acid complexes and disintegrate cellular structures. Guanidinium thiocyanate is especially strong protein denaturant because both the cation and anion disrupt the hydrophobic bonds between the amino acid side chains. RNA usually binds to proteins within a cell and this agent disassociates the nucleoprotein complex, without disrupting RNA structure. Thus RNA can be obtained by using these agents, after homogenisation and low-speed centrifugation and precipitated with ethanol. The protocol below explains the stepwise isolation of total RNA from cells and tissues using TRIzol reagent which is the mono-phasic solution of phenol and guanidine thiocyanate.
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Guanidinium chloride"

1

DEMENTIEVA, E. I., L. G. MALOSHENOK, and N. N. UGAROVA. "GUANIDINIUM CHLORIDE-INDUCED INACTIVATION OF FIREFLY LUCIFERASE AND ITS REACTIVATION." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0041.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Wiman, B., T. Carlsson, and J. Chmielewska. "EVIDENCE FOR A PLASMINOGEN ACTIVATOR INHIBITOR BINDING PROTEIN IN PLASMA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642859.

Full text
Abstract:
For several years it has been known that plasminogen activator inhibitor in plasma behaves as a high molecular weight compound on gelfiltration, in spite of that the molecular weight is only 50,000 in the presence of sodium dodecylsul-phate. The reason for this has so far been unknown. On gelfiltration of plasma, to which purified latent PAI from HT 1080 cells was added, the PAI antigen gel-filtered as a 50,000 Mr protein. However, if the latent form of PAI was reactivated by guanidinium chloride prior to the gel-filtra-tion experiment, an apparent molecular weight of about 250.000 for PAI antigen and activity was observed. If more than 10,000 U of PAI activity was added/mL of normal human plasma, excess PAI occurred at 50,000 Mr on gel-filtration. Human normalplasma was subjected to gel-filtration on sepha-cryl S-300 or Sepharose 6B and the fractions were checked for capacity to transform low Mr functional PAI to high Mr functional PAI. This capacity was only found in the 150 - 200,000 Mr region of the chromatogram. These data suggest that human plasma contains a protein that binds active forms of PAI. The complex of this protein and PAI could be dissociated by gelfiltration in the presence of 3 mol/L guanidinium chloride or 0.1 % (w/v) sodium dodecylsulphate. The physiological or pathophysiological role of the PAI-binding protein is not known. Work with purification of the protein is in progress. Considerable purification have so far been obtained by precipitation with polyethylenglycol 6000 (0-6%), gel-filtration on Sephacry1 S-300, followed by affinity chromatography on heparin-Sepharose.
APA, Harvard, Vancouver, ISO, and other styles
3

Samanta, Nirnay, Debasish Das Mahanta, and Rajib Kumar Mitra. "Urea and guanidinium chloride act as ‘water structure breakers’: The debate revisited by dielectric relaxation study in THz range." In 2015 40th International Conference on Infrared, Millimeter, and Terahertz waves (IRMMW-THz). IEEE, 2015. http://dx.doi.org/10.1109/irmmw-thz.2015.7327766.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Carlsson, I., J. Chmielewska, and B. Wiman. "ON DIFFERENT MOLECULAR EORMS OE PLASMINOGEN ACTIVATOR INHIBITOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644434.

Full text
Abstract:
The production of plasminogen activator inhibitor (PAI) by the human cell-lines Hep G2 and HT 1080 have been studied by immunochemical and functional methods. In conditioned medium collected after 2h, the PAI seemed to be almost fully active, but with increasing incubation time the activity was gradually lost, in spite of that the PAI-antigen content increased continously. The active PAI form can be separated from the inactive form by gel-filtration. The inactive form behaves as a low Mr (about 50,000) component in the absence and in the presence of sodium dodecyl-sulphate. In contrast, the active form of PAI behaves as a high Mr (>300,000) compound in the absence of sodium dodecylsulphate but as a low MT compound in its presence. The low M_r inactive PAI has been purified to homogeneity from HT 1080 conditioned medium, collected in the absence of fetal calf serum. This was achieved by chromatography on Concanavalin A-Sepharose, gel-filtration on Sephacryl S-300 and affinity chromatography on insolubilized monoclonal antibodies against PA-inhibitor. On treatment of this form of the inhibitor with 4 mol/L Guanidinium chloride, the activity was regained, but its gel-filtration behaviour was unchanged in the absence of serum/plasma (Mr about 50,000). Addition of plasma or serum prior to the gel-filtration, changed the elution pattern of PAI towards a high Mr form. The reason for this behaviour is not yet fully understood, but the most plausible explanation is the presence of a high Mr PAI-binding protein in plasma/serum. This hypothesis is presently being explored .
APA, Harvard, Vancouver, ISO, and other styles
5

Chmielewska, J., and B. Wiman. "ON THE KINETICS OF THE INHIBITION OF PLASMINOGEN ACTIVATORS BY THE PLASMINOGEN ACTIVATOR INHIBITOR PAI-1." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642808.

Full text
Abstract:
The kinetics of the inhibition of the following plasminogen activators: one- and two-chain tissue plasminogen activator (t-PA) and low and high molecular weight urokinase (UK) by PAI-1 was studied. For this purpose direct systems were employed and the reactions were studied in the presence of different concentrations of plasminogen activator chromogenic substrates. The second-order rate constant of the association reaction was estimated from the initial decline in plasminogen activator activity. Determination of the rate constants in the absence of substrates was performed by plotting the rate constants versus the substrate concentrations and extrapolation to zero concentration. The rate constants with all plasminogen activators were very similar and estimated as 2 - 4 x 107 M-1 x s-1. The reactions were also studied in the presence of 6-aminohexanoic acid, lysine, arginine, guanidinium chloride (final concentrations for all substances about 1 mmol/L) and heparin (10 mg/L), without any significant effect on the rate constants. The effect of soluble fibrin (bathroxobin-digested fibrinogen in urea) at 10 - 300 nmol/L was also studied. With one-chain t-PA the rate constant was decreased about 10-fold with the highest fibrin concentration and about 2-fold at 30 nmol/L. In contrast, the reactions with urokinase or two-chain t-PA were not influenced by fibrin at these concentrations. These findings may have a physiological significance: the one-chain t-PA adsorbed to the fibrin surface and actively involved in fibrinolysis would be protected against inactivation by PAI. This phenomenon adds further to the physiological fibrin specificity of one-chain t-PA.
APA, Harvard, Vancouver, ISO, and other styles
6

Wu, Q. Y., B. R. Bahnak, L. Coulombel, J. P. Caen, G. Pietu, and D. Meyer. "VON WILLEBRAND FACTOR mRNA IS SEVERELY REDUCED IN PIGS WITH HOMOZYGOUS VON WILLEBRAND DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644113.

Full text
Abstract:
Porcine von Willebrand disease (vWD), an autosomal recessive disorder, is similar to some of the severe forms of vWD in humans and is characterized by a prolonged bleeding time and very low or undetectable amounts of von Willebrand factor (vWF) antigen and activity in plasma, platelets and endothelial cells. The molecular events that control the lack of expression of vWF in the vWD pigs is not known and could be at the transcriptional or post-transcriptional level. Lungs from normal and two homozygous vWD pigs were extracted immediately after harvesting of the animals and placed on dry ice. Tissues were homogenized in 6 M guanidinium thiocyanate and RNA isolated by centrifugation through cesium chloride. Total RNA was analyzed by Northern hybridization including dénaturation in glyoxal, electrophoresis in 1.0 % agarose-2.2 M formaldehyde gels and transfer onto nitrocellulose. Messenger RNA was detected with a nick-translated human vWF cDNA probe or a human actin control probe. The vWF probe, cloned from a human lung library, was 2,280 bp in length and spanned nucleotides 960 to 3,240 of the human cDNA. These human probes were considered valid to detect levels of porcine vWF and actin mRNA because they hybridized with restriction enzyme digested genomic DNA from normal and vWD pig leucocytes under conditions of high stringency. The size of the vWF mRNA in the normal pigs after Northern hybridization was approximately 9.0 kb, similar to that of human vWF mRNA, and was easily detectable at the lowest concentration of RNA blotted (5 ug). In contrast, vWF mRNA from vWD pigs was at the lower limit of detection even at 10 ug of total RNA blotted. Nevertheless, although at extremely low levels, vWF mRNA from vWD pigs appeared to be the same size as the normal mRNA. These results agree with observations on the relationship of vWF secreted from 24 hr. cultures of endothelial cells from the pulmonary artery of normal and vWD pigs where the vWF levels were 0.90 and 0.06 U/108 cells, respectively. Therefore, it appears that the very low expression of vWF in the vWD pigs is due to a lack of transcription of the vWF gene. At this time, however, turnover of unstable transcripts in the vWD pigs can not be ruled out.
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Guanidinium chloride' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography