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Effect of protein disulfide isomerase on the regeneration of bovine ribonuclease A with dithiothreitol
Author(s) -
Shin Hang-Cheol,
Scheraga Harold A
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00946-1
Subject(s) - dithiothreitol , protein disulfide isomerase , ribonuclease , chemistry , bovine pancreatic ribonuclease , disulfide bond , biochemistry , regeneration (biology) , isomerase , native state , enzyme , rna , biology , microbiology and biotechnology , gene
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.