Ph-dependent proton absorption in chymotrypsin binding. Evidence for a ph-dependent conformation change of the enzyme

M L Bender et al. J Am Chem Soc. 1967.

. 1967 Jun 7;89(12):3052-4.

doi: 10.1021/ja00988a047.

No abstract available

Similar articles

Binding of competitive inhibitors to delta-chymotrypsin in the alkaline pH region. Competitive inhibition kinetics and proton-uptake measurements.
Valenzuela P, Bender ML. Valenzuela P, et al. Biochemistry. 1970 Jun 9;9(12):2440-6. doi: 10.1021/bi00814a008. Biochemistry. 1970. PMID: 5423263 No abstract available.
Conformation and activity of chymotrypsin: the pH-dependent, substrate-induced proton uptake.
McConn J, Ku E, Odell C, Czerlinski G, Hess GP. McConn J, et al. Science. 1968 Jul 19;161(3838):274-6. doi: 10.1126/science.161.3838.274. Science. 1968. PMID: 5657332
The binding of inhibitors to alpha-chymotrypsin at alkaline pH.
Johnson CH, Knowles JR. Johnson CH, et al. Biochem J. 1967 May;103(2):428-30. doi: 10.1042/bj1030428. Biochem J. 1967. PMID: 6032980 Free PMC article.
A proton-magnetic-resonance study of N-trifluoroacetyl-L-alanyl-L-phenylalaninal binding to alpha-chymotrypsin.
Wyeth P, Sharma RP, Akhtar M. Wyeth P, et al. Eur J Biochem. 1980 Apr;105(3):581-5. doi: 10.1111/j.1432-1033.1980.tb04535.x. Eur J Biochem. 1980. PMID: 6245886
Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relationships.
Fastrez J, Fersht AR. Fastrez J, et al. Biochemistry. 1973 Mar 13;12(6):1067-74. doi: 10.1021/bi00730a008. Biochemistry. 1973. PMID: 4688860 No abstract available.