Substrate hydrolysis by α-chymotrypsin under single-turnover conditions: The analysis of multi-stage biochemical kinetic processes by curve-stripping procedures
Author:
Publisher
Elsevier BV
Subject
Biochemistry
Reference8 articles.
1. Kinetics and mechanism of enzyme action: special reference to the determination of the number of intermediates in, and the effect of temperature on, enzyme catalysed reactions;Adams,1973
2. The kinetics and mechanism of the recombination reaction between apomyoglobin and haemin;Adams;Biochem. J.,1976
3. The effect of temperature on the individual stages of the hydrolysis of non-specific p-nitrophenol esters by α-chymotrypsin;Adams;Biochem. J.,1977
4. Optical and chemical identification of kinetic steps in trypsin and chymotrypsin catalysed reactions;Barman;Biochem. J.,1966
5. The correlation of the pH (pD) dependence and the stepwise mechanism of α-chymotrypsin catalysed reactions;Bender;J. Am. chem. Soc.,1964
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1. Single-turnover enzyme kinetics: The evaluation of rate constants from a single kinetic experiment;International Journal of Biochemistry;1977-01
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