Effect of protein disulfide isomerase on the regeneration of bovine ribonuclease A with dithiothreitol

FEBS Letters

Shin, Hang-Cheol¹  Scheraga, Harold A¹ 

[1] Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA

关键词: Protein disulfide isomerase;    Ribonuclease A;    Folding;    Dithiothreitol;    Distribution of intermediate;    RNAse A;    ribonuclease A;    PDI;    protein disulfide isomerase;    DTTox;    oxidized dithiothreitol;    DTTred;    reduced dithiothreitol;    AEMTS;    2-aminoethyl methanethiosulfonate;   

DOI  :  10.1016/S0014-5793(99)00946-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The role of protein disulfide isomerase (PDI) in the regeneration of ribonuclease A with dithiothreitol (DTT) was investigated at three different temperatures. The rates of formation of the native protein were markedly increased in the presence of PDI, 9-fold at 15°C, 6-fold at 25°C and 62-fold at 37°C, respectively. In the presence of PDI, major changes were found in the distribution of intermediates in the three-disulfide region at 25 and 15°C and also in the one-disulfide region at 15°C, with the fast accumulation of the two native-like species des-[65-72] and des-[40-95]. The present results indicate that PDI does not alter the two major parallel pathways involving des-[65-72] and des-[40-95] in the regeneration of ribonuclease A with DTT.

【 授权许可】

Unknown