DISULFIDE BOND IN CARBOXYPEPTIDASE A - A CHLORIDE ION NMR STUDY

被引：16

作者：

BRYANT, RG

YEH, HJC

STENGLE, TR

机构：

[1] Department of Chemistry, Stanford University, Stanford, CA

[2] Department of Chemistry, University of Massachusetts, Amherst, MA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1969年 / 37卷 / 04期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

D O I：

10.1016/0006-291X(69)90852-3

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：

Carboxypeptidase A was assayed for active sulfhydryl groups by titration with HgCl2. A chloride ion probe NMR technique was utilized to observe the behavior of the mercuric ion. Although mercuric ion was found to bind to the enzyme, it could be removed by dialysis showing that the binding cannot be through a sulfur atom. The absence of sulfhydryl groups indicates that the two half cystine residues in the molecule must be linked by a disulfide bond. © 1969.

引用

页码：603 / &

共 6 条

[1] COLEMAN JE, 1961, J BIOL CHEM, V236, P2244
[2] LIPSCOMB W, 1968, BROOKHAVEN SYM BIOL, P24
[3] HALIDE IONS AS PROBES FOR NUCLEAR MAGNETIC RESONANCE STUDIES OF PROTEINS . SULFHYDRYL GROUPS OF HEMOGLOBIN
STENGLE, TR
BALDESCHWIELER, JD
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1967, 89 (12) : 3045 - +
[4] HALIDE IONS AS CHEMICAL PROBES FOR NMR STUDIES OF PROTEINS
STENGLE, TR
BALDESCH.JD
[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1966, 55 (05) : 1020 - &
[5] VALLEE BL, 1960, J BIOL CHEM, V235, P64
[6] WALSH KA, 1962, P NATL ACAD SCI US, V58, P2220

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