Biochimica et biophysica acta, 953(3), 269-279 (1988-04-14)
The reaction of chymase, a chymotryptic proteinase from human skin, and bovine pancreatic chymotrypsin with a number of time-dependent inhibitors has been studied. An integrated equation, relating product formation with time, has been derived for the reaction of enzymes with
Inhibition of carboxypeptidase Y by chloromethyl ketone derivatives of benzyloxycarbonyl-L-phenylalanine.
R Hayashi et al.
Journal of biochemistry, 76(6), 1355-1357 (1974-12-01)
Protein science : a publication of the Protein Society, 4(11), 2433-2435 (1995-11-01)
The essential histidine residue of carboxypeptidase Y (CPY) was modified by a site-specific reagent, a chloromethylketone derivative of benzyloxycarbonyl-L-phenylalanine. The single modified histidine residue was converted to N tau-carboxy-methyl histidine (cmHis) upon performic acid oxidation. A peptide containing cmHis was
The effect of protease inhibitors N-tosyl-L-phenylalanine chloromethyl ketone (TPCK) and N-carbobenzoxy-L-phenylalanine chloromethyl ketone (ZPCK) at concentrations ranging from 1.5 x 10(-6) mol/l to 1.5 x 10(-4) mol/l on the specific binding of 3,5,3'-triiodothyronine (T3) to rat liver nuclear receptors was
Biogenesis of vaccina: interrelationship between post-translational cleavage, virus assembly, and maturation.
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