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首页> 外文期刊>Biochemistry >Isolation and Characterization of a Low-Molecular-Weight Immunoglobulin-Binding Protein from Yersinia pseudotuberculosis
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Isolation and Characterization of a Low-Molecular-Weight Immunoglobulin-Binding Protein from Yersinia pseudotuberculosis

机译：假性耶尔森氏菌低分子量免疫球蛋白结合蛋白的分离与鉴定

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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 deg C in the presence of SDS.
机译：已从假结核耶尔森氏菌细胞中分离出一种与细胞膜结合的低分子量免疫球蛋白结合蛋白（IBP）并进行了部分鉴定，该IBP是一种亲水性蛋白，具有55.3％的高极性指数，该蛋白的分子量经MALDI-TOF质谱测定为14.3 kD.CD光谱表明，IBP具有高含量的β-结构和无规卷曲结构，IBP含有甘氨酸作为N末端氨基酸，该蛋白质可以储存用于在碱性pH和中性pH值下会长时间聚集，但在碱性和中性pH下会聚集并失去活性.IBP结合兔IgG的最适pH值为6.0-7.5.IBP与Fc片段区域的IgG分子相互作用。在SDS存在下于100℃加热。

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