DETERMINATION OF THE MONOMER-DIMER EQUILIBRIUM OF INTERLEUKIN-8 REVEALS IT IS A MONOMER AT PHYSIOLOGICAL CONCENTRATIONS

被引：146

作者：

BURROWS, SD

DOYLE, ML

MURPHY, KP

FRANKLIN, SG

WHITE, JR

BROOKS, I

MCNULTY, DE

SCOTT, MO

KNUTSON, JR

PORTER, D

YOUNG, PR

HENSLEY, P

机构：

[1] SMITHKLINE BEECHAM PHARMACEUT, DEPT MOLEC IMMUNOL, KING OF PRUSSIA, PA 19406 USA

[2] SMITHKLINE BEECHAM PHARMACEUT, DEPT MACROMOLEC SCI, KING OF PRUSSIA, PA 19406 USA

[3] SMITHKLINE BEECHAM PHARMACEUT, DEPT PROT BIOCHEM, KING OF PRUSSIA, PA 19406 USA

[4] SMITHKLINE BEECHAM PHARMACEUT, DEPT GENE EXPRESS SCI, KING OF PRUSSIA, PA 19406 USA

[5] UNIV IOWA, DEPT BIOCHEM, IOWA CITY, IA 52242 USA

[6] NHLBI, CELLULAR BIOL LAB, BETHESDA, MD 20892 USA

来源：

BIOCHEMISTRY | 1994年 / 33卷 / 43期

关键词：

D O I：

10.1021/bi00209a002

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：

Interleukin-8 has been shown by X-ray crystallography and NMR to be a homodimer, suggesting that this is the form which binds to its receptor. Here we measure, for the first time, the monomer-dimer equilibrium of interleukin-8 using analytical ultracentrifugation and titration microcalorimetry and find that it dissociates readily to monomers with an equilibrium dissociation constant of 18 +/- 6 mu M at 37 degrees C. The present findings suggest that the monomer is the form which binds to the receptor. Comparison of experimental and structure-based calculated thermodynamics of interleukin-8 dimerization argues for limited subunit conformational changes upon dissociation to monomer.

引用

页码：12741 / 12745

页数：5

共 35 条

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Badea M G, 1979, Methods Enzymol, V61, P378

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