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- W1982176508 abstract "Creatine kinase is reversibly inhibited by incubation with S-nitrosothiols. Loss of enzyme activity is associated with the depletion of 5,5'-dithiobis (2-nitrobenzoic acid)-accessible thiol groups, and is not due to nitric oxide release from RSNO. Full enzymatic activity and protein thiol content are restored by incubation of the S-nitrosothiol-modified protein with glutathione. S-nitroso-N-acetylpenicillamine, which contains a more sterically hindered S-nitroso group than S-nitrosoglutathione, predominantly modifies the protein thiol to an S-nitrosothiol via a transnitrosation reaction. In contrast, S-nitrosoglutathione modifies creatine kinase predominantly by S-thiolation. Both S-nitroso-N-acetylpenicillamine and S-nitrosoglutathione modify bovine serum albumin to an S-nitroso derivative. This indicates that S-thiolation and S-nitrosation are both relevant reactions for S-nitrosothiols, and the relative importance of these reactions in biological systems depends on both the environment of the protein thiol and on the chemical nature of the S-nitrosothiol." @default.
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- W1982176508 date "2000-06-01" @default.
- W1982176508 modified "2023-09-23" @default.
- W1982176508 title "Modification of creatine kinase by S-nitrosothiols: S-nitrosation vs. S-thiolation" @default.
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- W1982176508 doi "https://doi.org/10.1016/s0891-5849(00)00281-1" @default.
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