Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin.

作者: I Björk , W W Fish

DOI: 10.1016/S0021-9258(18)34096-1

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参考文章(48)
J. Jesty, The kinetics of formation and dissociation of the bovine thrombin.antithrombin III complex. Journal of Biological Chemistry. ,vol. 254, pp. 10044- 10050 ,(1979) , 10.1016/S0021-9258(19)86670-X
Michael Laskowski, Robert W. Sealock, 11 Protein Proteinase Inhibitors-Molecular Aspects The Enzymes. ,vol. 3, pp. 375- 473 ,(1971) , 10.1016/S1874-6047(08)60402-3
R Rosenberg, D Beeler, R Jordan, Fractionation of low molecular weight heparin species and their interaction with antithrombin. Journal of Biological Chemistry. ,vol. 254, pp. 2902- 2913 ,(1979) , 10.1016/S0021-9258(17)30159-X
F Jordan, J A Patrick, S Salamone, Purine nucleoside phosphorylase cleaves the C--O bond of ribose 1-phosphate. Evidence from the 18O shift in 31P NMR. Journal of Biological Chemistry. ,vol. 254, pp. 2384- 2386 ,(1979) , 10.1016/S0021-9258(17)30233-8
R.E. Jordan, G.M. Oosta, W.T. Gardner, R.D. Rosenberg, The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin. Journal of Biological Chemistry. ,vol. 255, pp. 10081- 10090 ,(1980) , 10.1016/S0021-9258(19)70431-1
I Björk, C M Jackson, H Jörnvall, K K Lavine, K Nordling, W J Salsgiver, The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin. Journal of Biological Chemistry. ,vol. 257, pp. 2406- 2411 ,(1982) , 10.1016/S0021-9258(18)34938-X
Christopher. Walsh, Enzymatic Reaction Mechanisms ,(1978)
Birgitta NORDENMAN, Ake DANIELSSON, Ingemar BJORK, The Binding of Low‐Affinity and High‐Affinity Heparin to Antithrombin FEBS Journal. ,vol. 90, pp. 1- 6 ,(1978) , 10.1111/J.1432-1033.1978.TB12567.X
S.T. Olson, K.R. Srinivasan, I. Björk, J.D. Shore, Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction. Journal of Biological Chemistry. ,vol. 256, pp. 11073- 11079 ,(1981) , 10.1016/S0021-9258(19)68557-1