A monoclonal antibody selected for probing the folding of Staphylococcal nuclease and its N-terminal fragments

被引：2

作者：

Cheng, P ^{[1
]}

Zhou, JM

Guo, ZQ

机构：

[1] Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China

[2] Peking Univ, Life Sci Ctr, Beijing 100871, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 244卷 / 02期

关键词：

Staphylococcal nuclease; monoclonal antibody; protein folding; epitope;

D O I：

10.1006/bbrc.1997.8060

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：

Monoclonal antibody McAb2C9 against Staphylococcal nuclease (SNase R) and its N-terminal fragments was produced and characterized. It was observed that the intact enzyme SNase Il. and its seven fragments (SNR141, SNR135, SNR121, SNR110, SNR102, SNR79 and SNR52) differed in their interactions with McAb2C9. However, the fragments with weak immunoreactivity, such as SNR141 and SNR110, increased ability reacting with McAb2C9 in their partially unfolded state. It suggests that the differences of immunoreactivity among the fragments are due to diverse extent of the exposure of the specific epitope and the conformation of the peptide fragment. The monoclonal antibody McAb2C9 could be a useful probe to investigate the mechanism of folding of SNase R and its N-terminal fragments. (C) 1998 Academic Press.

引用

页码：556 / 560

页数：5

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