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
Biogenesis of vaccina: interrelationship between post-translational cleavage, virus assembly, and maturation.
The endoplasmic reticulum, or an organelle closely associated with it, contains proteases that can be used to remove partially assembled or improperly folded proteins. Very little is known at present about the types of protease that degrade these proteins. The
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)
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
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