Comparison of steady- and presteady-state kinetics of bovine and human plasmins
- 15 August 1972
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 11 (17), 3167-3171
- https://doi.org/10.1021/bi00767a005
Abstract
No abstract availableKeywords
This publication has 15 references indexed in Scilit:
- The Mechanism of the Inhibition of Plasmin Activity by ε-Aminocaproic AcidPublished by Elsevier ,1971
- [2] Titration of trypsin, plasmin, and thrombin with p-nitrophenyl p′-guanidinobenzoate HClPublished by Elsevier ,1970
- Studies on plasminogen. VIII. Species specificity of streptokinaseCanadian Journal of Biochemistry, 1969
- Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymesBiochemistry, 1969
- Direct Activation of Human Plasminogen by StreptokinaseExperimental Biology and Medicine, 1969
- The Determination of the Concentration of Hydrolytic Enzyme Solutions: α-Chymotrypsin, Trypsin, Papain, Elastase, Subtilisin, and Acetylcholinesterase1Journal of the American Chemical Society, 1966
- The Kinetics and Mechanism of Papain-Catalyzed Hydrolyses1Journal of the American Chemical Society, 1966
- Activity of Plasmin and Streptokinase-Activator on Substituted Arginine and Lysine EstersThrombosis and Haemostasis, 1966
- Mechanism of Action of Proteolytic EnzymesAnnual Review of Biochemistry, 1965
- Multiple Intermediates in Steady State Enzyme Kinetics.1,2 I. The Mechanism Involving a Single Substrate and ProductJournal of the American Chemical Society, 1959