Effect of methylation of the histidine residue in the active site of α‐chymotrypsin on the conformational stability of the enzyme
- 1 July 1972
- journal article
- Published by Wiley in FEBS Letters
- Vol. 23 (3) , 361-363
- https://doi.org/10.1016/0014-5793(72)80316-8
Abstract
No abstract availableKeywords
This publication has 6 references indexed in Scilit:
- Catalytic activity of α-chymotrypsin in which histidine-57 has been methylatedBiochemical Journal, 1971
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1970
- Methylation of histidine-57 in α-chymotrypsin by methyl ρ-nitrobenzenesulfonate. New approach to enzyme modificationBiochemistry, 1970
- Structure of crystalline α-chymotrypsinJournal of Molecular Biology, 1969
- Reversible filtration apparatus for concentrating protein solutions by the sephadex methodAnalytical Biochemistry, 1969
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969