1971 Volume 44 Issue 10 Pages 2801-2804
A cyclic hexapeptide, cyclo-(diglycyl-L-tyrosyl)2, was synthesized by several different routes; the cyclization reactions of a tripeptide active ester, a tripeptide azide, and a hexapeptide azide produced the desired cyclic hexapeptide. The cyclic peptide was hydrolyzed slowly by chymotrypsin to a tripeptide diglycyl-tyrosine, whereas a synthetic linear hexapeptide, diglycyl-L-tyrosyl-diglycyl-L-tyrosine, was hydrolyzed very rapidly to the tripeptide. Since the synthetic cyclo-(diglycyl-L-phenylalanyl)2 was insoluble in a buffer, it was not clear whether an incubation mixture of the substrate and enzyme yielded diglycyl-phenylalanine.
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