T. Yamamoto, N. Izumiya
Jun 1, 1966
Citations
0
Influential Citations
7
Citations
Quality indicators
Journal
Archives of biochemistry and biophysics
Abstract
Abstract A number of glycyl-aminoacyl- l -tyrosine ethyl esters, wherein the aminoacyl residues are glycyl, l -alanyl, β-alanyl, l -valyl, l -leucyl and l -norleucyl, have been synthesized and their susceptibility to the hydrolytic action of α-chymotrypsin was determined. The paper chromatographic and ninhydrin colorimetric analyses of the incubation mixture proved that the substrates are subjected to simple hydrolysis to the corresponding free tripeptides by the enzyme. By a comparison of the proteolytic coefficients, it could be shown that the relative rate of hydrolyses of the tripeptide esters is decreased markedly by the presence of a large side chain of the aminoacyl residue of substrate.