与原弹性蛋白相关的内在酶活性。

Intrinsic enzyme activity associated with tropoelastin.

作者信息

Mecham R P, Foster J A, Franzblau C

出版信息

Biochim Biophys Acta. 1976 Sep 28;446(1):245-54. doi: 10.1016/0005-2795(76)90115-x.

Abstract

The presence of an enzyme(s) associated with purified tropoelastin has been established. Results indicate that the enzyme(s) remains closely associated with the soluble elastin throughout the entire purification procedure suggesting that it is very tightly bound. Enzymatic activity is optimum through the pH range 7-9 (37 degrees C) and can be inhibited by disodium ethylenediaminetetraacetate, N-ethylmaleimide, sulfite, soybean trypsin inhibitor and human alpha-1-antitrypsin. The fragmentation pattern appears to be specific and reproducible.

摘要

已证实存在与纯化的原弹性蛋白相关的一种或多种酶。结果表明，在整个纯化过程中，该酶与可溶性弹性蛋白紧密结合，这表明它结合得非常紧密。酶活性在pH值7 - 9（37摄氏度）范围内最佳，并且可被乙二胺四乙酸二钠、N - 乙基马来酰亚胺、亚硫酸盐、大豆胰蛋白酶抑制剂和人α-1-抗胰蛋白酶抑制。片段化模式似乎具有特异性且可重复。