Monoclonal antibody, a novel probe for protein folding  

作　　者：程鹏 王锡德 静国忠 赵康源 周筠梅 郭振泉 

出　　处：《Science China(Life Sciences)》1998年第2期163-168,共6页中国科学（生命科学英文版）

基　　金：ProjectsupportedbytheNationalNaturalScienceFoundationofChina (GrantNo .396 80 0 0 2 )andClimbingProgramme.

摘　　要：Two monoclonal antibodies (McAb2C9, McAb1E5) against Staphylococcal nuclease R (SNase R) and its N terminal peptide fragments were prepared, purified and characterized. Further studies show that the intact enzyme SNase R and its seven N terminal peptide fragments differ in their interaction with McAb2C9. SNase R, SNR121, SNR102, SNR79 and SNR52 can bind to McAb2C9 readily, while fragments of SNR141, SNR135, SNR110 react with the antibody poorly. If this difference is due to diverse extent of exposure of the specific epitope in the fragments, it is suggested that the conformation of the peptide is subjected to continuous adjustments through chain elongation until the biologically active protein is formed. This result supports Tsou’s hypothesis of nascent peptide folding experimentally.Two monoclonal antibodies (McAb2C9, McAb1E5) against Staphylococcal nuclease R (SNase R) and its N terminal peptide fragments were prepared, purified and characterized. Further studies show that the intact enzyme SNase R and its seven N terminal peptide fragments differ in their interaction with McAb2C9. SNase R, SNR121, SNR102, SNR79 and SNR52 can bind to McAb2C9 readily, while fragments of SNR141, SNR135, SNR110 react with the antibody poorly. If this difference is due to diverse extent of exposure of the specific epitope in the fragments, it is suggested that the conformation of the peptide is subjected to continuous adjustments through chain elongation until the biologically active protein is formed. This result supports Tsou's hypothesis of nascent peptide folding experimentally.

关 键 词：STAPHYLOCOCCAL NUCLEASE MONOCLONAL antibody EPITOPE protein folding. 

分 类 号：Q813.2[生物学—生物工程]