Is Binding the Rate-limiting Step in Acylation of α-Chymotrypsin by Specific Substrates?
- 1 January 1973
- journal article
- Published by Springer Nature in Nature New Biology
- Vol. 241 (106) , 44
- https://doi.org/10.1038/newbio241044a0
Abstract
No abstract availableThis publication has 4 references indexed in Scilit:
- Magnetic resonance studies of protein-small molecule interactions. Dynamics of binding between N-trifluoroacetyl-D-tryptophan and .alpha.-chymotrypsinJournal of the American Chemical Society, 1972
- Application of transient nuclear magnetic resonance methods to the measurement of biological exchange rates. Interaction of trifluoroacetyl-D-phenylalanine with the chymotrypsinsJournal of the American Chemical Society, 1969
- Kinetic Evidence for the Formation of Acyl-Enzyme Intermediates in the α-Chymotrypsin-Catalyzed Hydrolyses of Specific SubstratesJournal of the American Chemical Society, 1964
- Steps in the formation and decomposition of some enzyme-substrate complexesDiscussions of the Faraday Society, 1955