An N‐hydroxylated peptide bond was found to be cleaved faster by an endopeptidase than
the corresponding peptide bond. This preferred enzymatic cleavage was detected during …

Peptide bonds involving the carbonyl group of amino acid residues with large hydrophobic
side chains are known to be easily hydrolyzed by 0tchymotrypsin. However, if the amido …

A number of peptide‐ester substrates of the general structure Ac‐Lxn‐. Lx2‐Lx1‐OMe have
been synthesized and their α‐chymotrypsin‐catalyzed hydrolysis studied. The kinetic …

Through the work of Balls and Jansen, 1 Oosterbaan, et a/., 2 and others, 3 it has been
established that a unique serine residue of-chymotrypsin is the ultimate site of acylation and …

The earlier investigations of o-chymotrypsin catalyzed hydrolysis of peptide substrates lead
to the conclusion that the peptide bonds on the carboxyl side of the amino acid residues …

Abstract The α-chymotrypsin [EC 3.4. 21.1]-catalyzed hydrolysis of peptide of the type Ac-X-
Glyn-NH2 (n= 0, 1, 2)(X: tryptophan (Trp), 2-(2-nitro-4-carboxyphenylsulfenyl)-tryptophan …

The enzymatic activity of α-chymotrypsin chemically modified with
monomethoxypolyethylene glycol (α-CT-PEG) is discussed using as test reactions the …

N-Maleyl-L-amino acid and peptide esters were synthesized and employed as substrates for
α-chymotrypsin. From the k cat/KM values can be suggested that benzyl esters are …

N-Hydroxymethylation of the N-terminal peptide bond in N-acetyl-L-phenylalanine amides
was found to protect the C-terminal amide bond against cleavage by α-chymotrypsin. The N …

The occurrence of a single reactive serine residue in several proteolytic enzymes has
indicated that the peptide sequences containing this reactiveserine are close to, or at, the …