Effect of protein disulfide isomerase on the regeneration of bovine ribonuclease A with dithiothreitol.
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 degrees C, 6-fold at 25 degrees C and 62-fold at 37 degrees 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 degrees C and also in the one-disulfide region at 15 degrees 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.
Shin
H C
HC
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
Scheraga
H A
HA
D000818:Animals; D002417:Cattle; D004229:Dithiothreitol / Q000378:metabolism*; D019704:Protein Disulfide-Isomerases / Q000378:metabolism* / Q000494:pharmacology; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism*; D013696:Temperature
D012259:Ribonuclease, Pancreatic; D019704:Protein Disulfide-Isomerases; D004229:Dithiothreitol