| Literature DB >> 4966474 |
Abstract
GSH, but not GSSG, inhibits the reactivation by phosphate ion of ribonuclease activity inactivated by urea or guanidine. The effects of GSH are rather slow and pretreatment of ribonuclease with urea is a requisite for the inhibitory action of GSH on enzyme reactivation. GSH is more effective in urea than in guanidine and its action is greatly enhanced by EDTA. An optimum pH of about 9.0 was found for the inhibitory effect of GSH. Titration of the thiol groups formed after inactivation of ribonuclease by GSH strongly suggests that the reduction of only one disulphide linkage is involved. The reduction of this bond is sufficient to completely abolish the enzymic activity.Entities:
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Year: 1968 PMID: 4966474 PMCID: PMC1198562 DOI: 10.1042/bj1060707
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857