Äîêóìåíò âçÿò èç êýøà ïîèñêîâîé ìàøèíû. Àäðåñ îðèãèíàëüíîãî äîêóìåíòà : http://www.mce.biophys.msu.ru/archive/doc57352/doc.pdf
Äàòà èçìåíåíèÿ: Tue Mar 9 12:27:13 2010
Äàòà èíäåêñèðîâàíèÿ: Mon Oct 1 22:45:41 2012
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. 1503­1514. . .,

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. 2000. . 65, 8. . 976­985. Bernfield M., Gotte M., Park P.W., Reizes O., Fitzgerald ML, Lincecum J, Zako M. Functions of cell surface heparan sulfate proteoglycans // Annu Rev Biochem. 1999. Vol. 68. P. 729­777. Himmel H.M., Pietsch M., Streller U., Graf E.M., Ravens U. Changes in morphology and inward rectifier currents in human atrial myocytes depend on culture 2002. Vol. 97, no. 6. P. 434­44. conditions // Basic Res Cardiol. Babu K.R., Douglas D.J. Changes in morphology and inward rectifier currents in human atrial myocytes depend on culture conditions // Biochemistry. 2000. Vol. 39, no. 47. P. 14702­14710. Bhowmick R., Jagannadham M.V. Multiple Intermediate Conformations of Jack Bean Urease at Low pH: Anion-induced Refolding // Protein J. 2006. Vol. 25, no. 6. P. 399­410. Follmer C., Real-Guerra R., Wasserman Olivera-Severo D., Carlini C.R. Jackbean, soybean and Bacillus pasteurii ureases: biological effects unrelated to ureolytic activity // Eur.J. Biochem. 2004. Vol. 271. P. 1357­1363. Follmer C., Barcellos G.B, Zingali R.B.,MachadoO.L., Alves E.W., Barja-Fidalgo C., GuimarÖes J.A., Carlini C.R. Canatoxin, a toxic protein from jack beans (Canavalia ensiformis), is a variant form of urease (EC 3.5.1.5): biological effects of urease independent of its ureolytic activity // Biochem. J. 2001. Vol. 360. P. 217­224. Hausinger R.P., and Karplus P.A. in Handbook of Metalloproteins (Wieghardt, K., Huber R., Poulos T.L. and Messerschmid A.). U.K.: Wiley & Sons, Ltd., West Sussex. P. 867­879. Jabri E., Carr M.B., Hausinger R.P., Karplus P.A. The Crystal Structure of Urease from Klebsiella Aerogenes // Science. 1995. Vol. 268. P. 998­1004. Kaibara K, Okazaki T, Bohidar HB, Dubin PL. pH-Induced Coacervation in Complexes of Bovine Serum Albumin and Cationic Polyelectrolytes // Biomacromolecules. 2000. Vol. 1. P. 100­107. Mulrooney S. Conformational dynamics of E. coli thioredoxin reductase: identification of two catalytically important states by ultra-fast flavin fluorescence spectroscopy // Archiv. Biochem Biphys. 2001. Vol. 394. P. 280­282. Woody R.W. Circular Dichroism // Methods in Enzymology. 1995. Vol. 246. P. 45.
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POLYELECTROLYTE-PROTEIN COMLEX. POLYALLYLAMIN INFLUENCE ON STUCTURE AND FUNCTIONS OF UREASE Durdenko E. V., Dybovskaya Yu. N., Tichonenko S. A., Saburova E. A.

Influence of polyelectrolyte polyallylamine (PAH) on structure and catalytic characteristics of urease (Canavalia ensiformis) by methods steady-state kinetics, fluorescence and circular dichroism spectroscopy is studied. It is shown that this polyelectrolyte is strong inhibitor of urease (50 % inhibition of enzyme with concentration PAH of 0,5 mkg/ml at neutral values ). It is assumed regulatory role specific cation-binding sites on a molecule urease, defining structural dynamics a complex enzyme-polyelectrolyte.

157