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140 related items for PubMed ID: 1213984

  • 1. Substituent effects on substrate activation and Michaelis-Menten Kinetic parameters in the alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetates.
    Shimamoto N, Fukutome H.
    J Biochem; 1975 Oct; 78(4):663-71. PubMed ID: 1213984
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  • 2. A method for analyzing enzyme kinetics with substrate activation and inhibition and its application to the alpha-chymotrypsin-catalyzed hydrolysis of phenyl acetates.
    Shimamoto N.
    J Biochem; 1976 Nov; 80(5):961-8. PubMed ID: 1002688
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  • 4. Kinetic study of alpha-chymotrypsin catalysis with regard to the interaction between the specificity-determining site and the aromatic side chain of substrates.
    Ohno M, Sato S, Karasaki Y, Tsukamoto S.
    J Biochem; 1976 Aug; 80(2):239-51. PubMed ID: 1002668
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  • 12. Pressure effects on substrate activation phenomena in the alpha-chymotrypsin-catalyzed hydrolysis of p-nitrophenyl acetate.
    Makimoto S, Taniguchi Y.
    Biochim Biophys Acta; 1988 Jun 13; 954(3):343-6. PubMed ID: 3370219
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  • 13. Proteinase K from the mold Tritirachium album Limber. Specificity and mode of action.
    Kraus E, Femfert U.
    Hoppe Seylers Z Physiol Chem; 1976 Jul 13; 357(7):937-47. PubMed ID: 992572
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  • 18. The kinetics of hydrolysis of some extended N-aminoacyl-L-phenylalanine methyl esters by bovine chymotrypsin A-alpha. Evidence for enzyme subsite S5.
    Hill CR, Tomalin G.
    Biochim Biophys Acta; 1981 Jul 24; 660(1):65-72. PubMed ID: 7272314
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  • 19. pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method.
    Fersht AR, Renard M.
    Biochemistry; 1974 Mar 26; 13(7):1416-26. PubMed ID: 4819756
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