ION BINDING BY ALPHA-CHYMOTRYPSIN

被引：10

作者：

FRIEDBERG, F

BOSE, S

机构：

[1] Howard University, Departments of Biochemistry, Departments of Chemistry, Washington

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 06期

关键词：

D O I：

10.1021/bi00834a045

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 binding of Na+, Ca2+, Cl-, and SO2-4 by deionized α-chymotrypsin was investigated as a function of pH at 25° with the use of permselective membrane electrodes. The enzyme has an affinity for all these ions even close to the isoionic point but it holds more cations than anions. Graphs of ̄v/c with respect to ̄v give linear relationships for these four ions and apparent maximum number of binding sites as well as apparent association constants are deduced from such plots. © 1969, American Chemical Society. All rights reserved.

引用

页码：2564 / +

页数：1

共 12 条

[1] STUDIES ON THE BINDING OF SMALL IONS IN PROTEIN SOLUTIONS WITH THE USE OF MEMBRANE ELECTRODES .4. THE BINDING OF CALCIUM IONS IN SOLUTIONS OF VARIOUS PROTEINS [J].