原弹性蛋白的蛋白水解作用。

Proteolysis of tropoelastin.

作者信息

Mecham R, Foster J A, Franzblau C

出版信息

Adv Exp Med Biol. 1977;79:209-20. doi: 10.1007/978-1-4684-9093-0_18.

Abstract

The presence of an enzyme associated with tropoelastin is described. The enzyme has a pH optimum between 7 and 9 and trypsin-like specificity. Upon incubation, tropoelastin (72,000 molecular weight) is cleaved into relatively high molecular weight fragments. In addition to the parent molecule, five discrete polypeptide bands are usually observed on SDS gels with molecular weights of approximately 57,000, 45,000, 36,000, 25,000 and 13-14,000.

摘要

描述了一种与原弹性蛋白相关的酶。该酶的最适pH值在7至9之间，具有类胰蛋白酶特异性。孵育后，原弹性蛋白（分子量72,000）被切割成相对高分子量的片段。除了亲本分子外，在SDS凝胶上通常观察到五条离散的多肽带，分子量约为57,000、45,000、36,000、25,000和13 - 14,000。