CIRCULAR DICHROISM SPECTRA OF COMPLEXES OF 1-ANILINO-8-NAPHTHALENESULFONATE WITH BOVINE SERUM ALBUMIN . EVIDENCE FOR HETEROGENEITY OF BINDING

被引：22

作者：

ANDERSON, SR

机构：

[1] Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 12期

关键词：

D O I：

10.1021/bi00840a028

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 adsorption of 1-anilino-8-naphthalenesulfonate by bovine serum albumin induces asymmetry in the ligand molecule. The sign and magnitude of the resulting circular dichroic bands vary with the average degree of saturation of the protein with ligand. Matrix rank analysis of the data demonstrates two spectrally distinguishable components within the set of five primary binding sites. The accurate differential measurements obtained in circular dichroism reflect heterogeneity undetectable in direct determinations of protein-ligand equilibria. © 1969, American Chemical Society. All rights reserved.

引用

页码：4838 / &

共 13 条

[1] FLUORESCENCE POLARIZATION OF COMPLEXES OF 1-ANILINO-8-NAPHTHALENESULFONATE WITH BOVINE SERUM ALBUMIN . EVIDENCE FOR PREFERENTIAL ORIENTATION OF LIGAND [J].