蛤α-副肌球蛋白的广泛羧肽酶消化。对残留蛋白质大小和溶解性的影响。

Extensive carboxypeptidase digestion of clam alpha-paramyosin. The effect on the size and solubility of the residual protein.

作者信息

Cordes D A, Cowgill R W

出版信息

Biochim Biophys Acta. 1979 Apr 25;577(2):410-4. doi: 10.1016/0005-2795(79)90045-x.

Abstract

The purpose of this paper is to provide further evidence that the C-terminal 1/3 of the alpha-paramyosin molecule is the portion responsible for the low solubility of alpha-paramyosin at neutral pH and low ionic strength. This was accomplished by digesting from the C-terminal end with carboxypeptidases A and B in 2 M urea at pH 8.5. The solubility increased as the molecular weight decreased until a stable segment 2/3 of the size of the molecule remained.

摘要

本文的目的是提供进一步的证据，证明α-副肌球蛋白分子的C末端1/3是导致α-副肌球蛋白在中性pH值和低离子强度下低溶解度的部分。这是通过在pH 8.5的2 M尿素中用羧肽酶A和B从C末端进行消化来实现的。随着分子量的降低，溶解度增加，直到分子大小的稳定片段2/3保留下来。