一种用于探测葡萄球菌核酸酶及其N端片段折叠情况而筛选出的单克隆抗体。

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

作者信息

Cheng P, Zhou J M, Guo Z Q

机构信息

National Lab of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, People's Republic of China.

出版信息

Biochem Biophys Res Commun. 1998 Mar 17;244(2):556-60. doi: 10.1006/bbrc.1997.8060.

DOI:10.1006/bbrc.1997.8060

PMID:9514853

Abstract

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 R 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.

摘要

制备并鉴定了抗葡萄球菌核酸酶（SNase R）及其N端片段的单克隆抗体McAb2C9。观察到完整的酶SNase R及其七个片段（SNR141、SNR135、SNR121、SNR110、SNR102、SNR79和SNR52）与McAb2C9的相互作用存在差异。然而，免疫反应性较弱的片段，如SNR141和SNR110，在其部分展开状态下与McAb2C9反应的能力增强。这表明片段之间免疫反应性的差异是由于特定表位暴露的程度和肽片段构象的不同所致。单克隆抗体McAb2C9可能是研究SNase R及其N端片段折叠机制的有用探针。