The Interaction between Chymotrypsin and Horse Leucocyte Neutral Proteinases Inhibitor
- 1 January 1981
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 362 (2) , 1345-1350
- https://doi.org/10.1515/bchm2.1981.362.2.1345
Abstract
The inhibition of .alpha.-chymotrypsin by horse leukocyte neutral proteinases inhibitor was time-dependent with synthetic substrate N-benzoyl-L-tyrosine ethyl ester but not with azo-casein. This time dependent could be used to calculate the rate constant Kass for the association of the inhibitor with bovine .alpha.-chymotrypsin (Kass = 0.3 .times. 106 M-1 s-1). The inhibitor reacted with chymotrypsin at a molar ratio of 1:1. The dissociation constant Ki = 0.30 .times. 10-9 M of the complex indicates a very strong interaction between enzyme and inhibitor.This publication has 13 references indexed in Scilit:
- Human‐Polymorphonuclear‐Leucocyte Neutral Protease and Its InhibitorEuropean Journal of Biochemistry, 1976
- A kinetic study of the inhibition of human and bovine trypsins and chymotrypsins by the inter-α-inhibitor from human plasmaBiochimica et Biophysica Acta (BBA) - Enzymology, 1976
- Neutral proteinases of human spleen. Purification and criteria for homogeneity of elastase and cathepsin GBiochemical Journal, 1976
- Inhibition of the Elastase-Like Esterase in Human Leukocyte Granules by Human Leukocyte Cell SapExperimental Biology and Medicine, 1971
- A MODIFIED SPECTROPHOTOMETRIC DETERMINATION OF CHYMOTRYPSIN, TRYPSIN, AND THROMBINCanadian Journal of Biochemistry and Physiology, 1959
- The determination of enzyme inhibitor constantsBiochemical Journal, 1953
- Pancreatic trypsin inhibitor. 2. Reaction with trypsinBiochemical Journal, 1953
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934