Dissociation of the thrombin/antithrombin III reaction from amidolytic activity of the enzyme at high salt concentration

Thrombosis Research
G Oshima


Amidolytic activity of thrombin increased proportionally with NaCl concentrations up to 1 M NaCl, due to an increase in the turnover rate with no change in the Km of the enzyme. Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations. Moreover, ratio of rates of the amidolytic activity of thrombin to of the enzyme/AT III reaction was not constant at several pHs. The rate of the thrombin/AT III reaction appeared to be inversely correlated with the enzyme's stability. Therefore, it was concluded that some factor(s) other than the active site of the thrombin molecule was more important in its primary interaction with AT III.


Jul 21, 1978·Biochimica Et Biophysica Acta·M W Pomerantz, W G Owen
Aug 1, 1976·Archives of Biochemistry and Biophysics·B LahiriR W Colman
Sep 16, 1975·Biochemical and Biophysical Research Communications·R L LundbladK G Mann
Jul 1, 1987·Thrombosis Research·G Oshima, K Nagasawa
Feb 1, 1988·Thrombosis Research·G Oshima
Sep 1, 1988·Chemical & Pharmaceutical Bulletin·G Oshima
Aug 20, 1986·Journal of Molecular Biology·T ImotoT Ueda
Aug 15, 1984·Archives of Biochemistry and Biophysics·G OshimaM Yamada
Feb 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·G M OostaR D Rosenberg
Feb 1, 1981·The Biochemical Journal·A Danielsson, I Björk

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May 15, 1990·Thrombosis Research·G Oshima

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