A Soluble protein derived from elastin

Abstract

DURING an investigation of the early stages of hydrolysis of various mucoids and connective-tissue proteins, it was observed that, on partial hydrolysis with acetic acid or oxalic acid at 100°, aspartic acid was in each case the first amino-acid to appear in the free condition, followed at a somewhat later stage by glutamic acid1. Since elastin has an unusually low content of the dicarboxylic amino-acids2, it was thought that, with this protein, hydrolytic cleavage at some proportion of the aspartic or glutamic acid residues might yield soluble degradation products of high molecular weight. © 1951 Nature Publishing Group.