A kinetic investigation of subsites S1′ and S2′ in α-chymotrypsin and subtilisin BPN′
- 1 January 1977
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 178 (1) , 188-194
- https://doi.org/10.1016/0003-9861(77)90183-7
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. Stereochemical interpretationBiochemistry, 1973
- Subtilisin. Stereochemical mechanism involving transition-state stabilizationBiochemistry, 1972
- A model for the association of bovine pancreatic trypsin inhibitor with chymotrypsin and trypsinJournal of Molecular Biology, 1972
- X-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPNBiochemistry, 1972
- Kinetic investigation of the crystallographically deduced binding subsites of bovine chymotrypsin AγBiochemistry, 1972
- Substrate binding site in bovine chymotrypsin Aγ. Crystallographic study using peptide chloromethyl ketones as site-specific inhibitorsBiochemistry, 1971
- Subtilisin BPN′: Kinetic study with oligopeptidesArchives of Biochemistry and Biophysics, 1970
- Comparison of α-chymotrypsin and subtilisin BPN1: Size and specificity of the active siteBiochemical and Biophysical Research Communications, 1969
- The determination of amino-acids with ninhydrinThe Analyst, 1955