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Change in the conformation of δ‐chymotrypsin upon binding a specific substrate at high pH

Data up to Jan 2025

Published1975
Citations2
References16

Total Citations Per Year

Abstract

References (16)

PHOTOMETRIC NINHYDRIN METHOD FOR USE IN THE CHROMATOGRAPHY OF AMINO ACIDS

1948 • 2,986 citations

Conformational equilibria in α- and δ-chymotrypsin

1972 • 250 citations

Implication of an Ionizing Group in the Control of Conformation and Activity of Chymotrypsin

1966 • 193 citations

ACYLATION OF THE ENZYMATIC SITE OF δ-CHYMOTRYPSIN BY ESTERS, ACID ANHYDRIDES, AND ACID CHLORIDES

1957 • 155 citations

Studies of the activity of chymotrypsin

1970 • 108 citations

Investigations of the Chymotrypsin-catalyzed Hydrolysis of Specific Substrates

1967 • 82 citations

Conformation of the high pH form of chymotrypsin

1969 • 69 citations

Binding interactions between two ligands and a monomeric protein

1970 • 40 citations

Activity and conformation of the alkaline form of δ-chymotrypsin studied by the specific acylation of isoleucine-16

1970 • 38 citations

Conformation and Activity of Chymotrypsin: The p H-Dependent, Substrate-Induced Proton Uptake

1968 • 31 citations

Binding of competitive inhibitors to δ-chymotrypsin in the alkaline pH region. Competitive inhibition kinetics and proton-uptake measurements

1970 • 30 citations

Identification of the ionising group controlling the active conformation of δ-chymotrypsin in alkaline pH

1967 • 23 citations

The Time Dependence of the Activity of δ‐Chymotrypsin at High pH

1973 • 17 citations

Rate of ligand-promoted isomerization of proteins. Relaxation study of the “alkaline-transition” of δ-chymotrypsin

1971 • 17 citations

APPENDIX

1970 • 6 citations

Coupling of slow processes to steady state reactions.

1970 • 5 citations

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Change in the conformation of δ‐chymotrypsin upon binding a specific substrate at high pH (1975) – FEBS Letters | Metascience Observatory Explorer