THE ACETYLATION OF THROMBIN
- 1 January 1959
- journal article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry and Physiology
- Vol. 37 (1), 1361-1366
- https://doi.org/10.1139/y59-150
Abstract
Purified thrombin-C loses its clotting power upon acetylation. The thrombin-E which is produced during the acetylation has approximately twice the proteolytic activity as the original thrombin-C. Evidently amino groups are not necessary to have thrombin-E activity, but if o-acyl groups are also produced the enzyme does not hydrolyze p-toluenesulphonylarginine methyl ester (TAMe). The activity can be recovered by spontaneous hydrolysis of the o-acyl groups at pH 8.5. Thrombin-E does not activate fibrinogen, but does lyse fibrin. The optimum pH with TAMe as substrate is 8.8. It may be that thrombin-C is a dimer of the basic structure in thrombin-E.Keywords
This publication has 12 references indexed in Scilit:
- Esterase and Clotting Activity Derived From Purified ProthrombinAmerican Journal of Physiology-Legacy Content, 1957
- Further Studies of Prothrombin Derivatives.Experimental Biology and Medicine, 1957
- On the mechanism of enzyme action. LXIII. Specificity of acetylation of proteins with C14 anhydrideArchives of Biochemistry and Biophysics, 1957
- A MODIFIED NINHYDRIN REAGENT FOR THE PHOTOMETRIC DETERMINATION OF AMINO ACIDS AND RELATED COMPOUNDSJournal of Biological Chemistry, 1954
- THE ACTION OF THROMBIN ON SYNTHETIC SUBSTRATESJournal of Biological Chemistry, 1954
- Fibrinolytic Activity of Purified ThrombinScience, 1950
- SOME PROPERTIES OF PURIFIED PROTHROMBIN AND ITS ACTIVATION WITH SODIUM CITRATEBlood, 1950
- THE REACTION OF ACETYLCHOLINE AND OTHER CARBOXYLIC ACID DERIVATIVES WITH HYDROXYLAMINE, AND ITS ANALYTICAL APPLICATIONJournal of Biological Chemistry, 1949
- FACTORS WHICH INFLUENCE THE ACTIVITY OF PURIFIED THROMBINAmerican Journal of Physiology-Legacy Content, 1942