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An essential role of cytosolic thioltransferase in protection of pyruvate kinase from rabbit liver against oxidative inactivation
Author(s) -
Axelsson Kent,
Mannervik Bengt
Publication year - 1983
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(83)80494-3
Subject(s) - glutathione , cytosol , chemistry , glutathione reductase , biochemistry , glutaredoxin , oxidative phosphorylation , pyruvate kinase , rabbit (cipher) , pyruvate dehydrogenase kinase , enzyme , glycolysis , pyruvate dehydrogenase complex , glutathione peroxidase , statistics , mathematics
Pyruvate kinase from rabbit liver is inactivated spontaneously in the presence of air. Glutathione in physiological concentrations gives partial protection against inactivation. Full protection is obtained with glutathione and purified cytosolic thioltransferase supplemented with a glutathione‐regenerating system. It is suggested that thioltransferase plus glutathione serve a general function in protecting protein thiol groups against oxidation.

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