EXTENSIVE CARBOXYPEPTIDASE DIGESTION OF CLAM ALPHA-PARAMYOSIN - EFFECT OF THE SIZE AND SOLUBILITY OF THE RESIDUAL PROTEIN

被引：1

作者：

CORDES, DA

COWGILL, RW

机构：

[1] Department of Biochemistry, Bowman Gray School of Medicine, Wake Forest University, Winston-Salem

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 577卷 / 02期

关键词：

(Clam); Carboxypeptidase digestion; Muscle protein; Protein solubility; α-Paramyosin cleavage;

D O I：

10.1016/0005-2795(79)90045-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The purpose of this paper is to provide further evidence that the C-terminal 1 3 of the α-paramyosin molecule is the portion responsible for the low solubility of α-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. © 1979.

引用

页码：410 / 414

页数：5

共 13 条

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[9] COMPARISON OF MUSCLE PROTEIN PARAMYOSIN FROM DIFFERENT MOLLUSCAN SPECIES
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