Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 769 - 776, Juni 1976 Hydrolysis-Resy n thesis Equilibrium of the Lysine-15--Alanine-16 Peptide Bond in Bovine Trypsin Inhibitor (Kunitz) Harald TSCHESCHE and Sigrid KUPFER Organisch-Chemisches Institut der Technischen Universität München Lehrstuhl für Organische Chemie und Biochemie (Received 13 April 1976) Dedicated to Prof. H. Zahn on the occasion of his 60th birthday Summary: Catalytic amounts of bovine ß-trypsin, equilibrium concentrations of virgin and modified bovine -chymotrypsin and porcine plasmin inhibitor are established by plasmin after almost establish a true thermodynamic equilibrium 300 days starting from either pure virgin or pure 15 16 between virgin (I) (reactive site Lys -Ala modified inhibitor. Thus, the hydrolysis constant peptide bond intact) and modified (I*) (this bond ^Hyd = [!*]/[!] is determined to be 0.33 at pH 5.O. In spite of many unsuccessful attempts, hydrolyzed) bovine trypsin/kallikrein inhibitor this demonstrates that the reactive site peptide (Kunitz). The very slow reaction rates for attainbond Lys15-Ala16 in the bovine trypsin inhibitor ing equilibrium are pH-dependent and differ for different enzymes. Optimal rates are for ß-trypsin (Kunitz) can be hydrolyzed by catalytic amounts at pH 3.75, for -chymotrypsin at pH 5.5, and for of endopeptidase. It further confirms
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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