Isolation and characterization of a low-molecular-weight immunoglobulin-binding protein from Yersinia pseudotuberculosis

被引：6

作者：

Sidorin, E. V. ^{[1
]}

Kim, N. Yu. ^{[1
]}

Leichenko, E. V. ^{[1
]}

Anastyuk, S. D. ^{[1
]}

Dmitrenok, P. S. ^{[1
]}

Naberezhnykh, G. A. ^{[1
]}

Solov'eva, T. F. ^{[1
]}

机构：

[1] Russian Acad Sci, Pacific Inst Bioorgan Chem, Far Eastern Div, Vladivostok 690022, Russia

来源：

BIOCHEMISTRY-MOSCOW | 2006年 / 71卷 / 11期

关键词：

immunoglobulin G; Fc-fragment of IgG; immunoglobulin-binding protein;

D O I：

10.1134/S0006297906110149

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：

A low-molecular-weight immunoglobulin-binding protein (IBP) bound with the cell envelope has been isolated from Yersinia pseudotuberculosis cells and partially characterized. This IBP is a hydrophilic protein with a high polarity index of 55.3%. The molecular weight of the protein has been determined by MALDI-TOF mass spectrometry as 14.3 kD. CD spectroscopy showed that the IBP has high contents of the beta-structure and random coil structure. The IBP contains glycine as the N-terminal amino acid. The protein can be stored for a long time at acidic pH values but aggregates and loses activity at alkaline and neutral pH. The IBP binds rabbit IgG with optimum at pH of 6.0-7.5. The IBP interacts with IgG molecule in the Fc-fragment region. The protein retains activity after heating at 100 degrees C in the presence of SDS.

引用

页码：1278 / 1283

页数：6

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