CHARACTERIZATION OF SELF-ASSOCIATION OF A SOYBEAN PROTEINASE INHIBITOR BY MEMBRANE OSMOMETRY

被引：30

作者：

HARRY, JB

STEINER, RF

机构：

[1] Laboratory of Physical Biochemistry, Naval Medical Research Institute, National Naval Medical Center, Bethesda

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 12期

关键词：

D O I：

10.1021/bi00840a057

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 self-association of a soybean trypsin and chymotrypsin inhibitor has been characterized by membrane osmometry. The association is found to be of the monomer ⇌ dimer type with little or no higher forms present. The extent of association increases with increased ionic strength and with decreased monomer charge. The ionic strength effect and the pH effect (below pH 6) are both found to be consistent with the theoretical electrostatic free-energy changes. © 1969, American Chemical Society. All rights reserved.

引用

页码：5060 / &

共 16 条

[11]

LANGE NA, 1967, LANGES HANDBOOK CHEM, P1216

[12]

MILLAR DBS, 1969, J BIOL CHEM, V244, P281

[13] EXPERIMENTAL ASPECTS OF HIGH-SPEED MEMBRANE OSMOMETER [J].

PAGLINI, S .

ANALYTICAL BIOCHEMISTRY, 1968, 23 (02) :247-&

[14]

STAVERMAN AJ, 1951, RECL TRAV CHIM PAY B, V70, P344

[15] REVERSIBLE ASSOCIATION PROCESSES OF GLOBULAR PROTEINS .5. THE STUDY OF ASSOCIATING SYSTEMS BY THE METHODS OF MACROMOLECULAR PHYSICS [J].

STEINER, RF .

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1954, 49 (02) :400-416

[16]

VERWEY EJ, 1958, THEORY STABILITY LYP

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