Kinetic analysis by stopped-flow radiationless energy transfer studies: effect of anions on the activity of carboxypeptidase A
- 14 January 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (1) , 94-100
- https://doi.org/10.1021/bi00349a014
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 18 references indexed in Scilit:
- Stopped-flow radiationless energy transfer kinetics: direct observation of enzyme-substrate complexes at steady stateBiochemistry, 1980
- Low temperature stopped-flow spectrometryAnalytical Biochemistry, 1980
- Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogue.Proceedings of the National Academy of Sciences, 1980
- Enzymic dynamics and molecular orbital study on the roles of arginines in carboxypeptidase A, a sliding mechanismJournal of the American Chemical Society, 1978
- Kinetic properties of crystalline enzymes. Carboxypeptidase ABiochemistry, 1977
- Purification and crystallization of human carboxypeptidase ABiochemistry, 1976
- The Enzymic Behavior of Carboxypeptidase-A in the Solid State*Biochemistry, 1966
- THE EFFECT OF ANIONS ON THE ACTIVITY OF CARBOXYPEPTIDASEJournal of Biological Chemistry, 1950
- THE CHEMICAL NATURE AND MODE OF ACTION OF PANCREATIC CARBOXYPEPTIDASEJournal of Biological Chemistry, 1949
- PANCREATIC CARBOXYPEPTIDASE; A METAL PROTEINJournal of Biological Chemistry, 1948