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The effect of 2,4,6‐trinitrobenzenesulfonate on mercuric reductase, glutathione reductase and lipoamide dehydrogenase
Author(s) -
Carlberg Inger,
Sahlman Lena,
Mannervik Bengt
Publication year - 1985
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 - 10.1016/0014-5793(85)80240-4
Subject(s) - glutathione reductase , reductase , chemistry , biochemistry , glutathione , enzyme , glutathione peroxidase
Among the three closely related enzymes, lipoamide dehydrogenase, mercuric reductase, and glutathione reductase only the latter is inhibited by 2,4,6‐trinitrobenzenesulfonate (TNBS). On the other hand, all three enzymes exhibit high rates of TNBS‐dependent NADPH oxidation. In the case of glutathione reductase and mercuric reductase this TNBS‐dependent activity displays substrate inhibition by excess of NADPH and is strongly stimulated by NADP + . The stimulation is especially pronounced with mercuric reductase, 25‐fold under some conditions. Neither substrate inhibition nor stimulation by NAD + is observed with lipoamide dehydrogenase.