Rat glutathione transferase 8‐8, an enzyme efficiently detoxifying 4‐hydroxyalk‐2‐enals

FEBS Letters

Guthenberg, Claes¹  Ålin, Per¹  Jensson, Helgi¹  Mannervik, Bengt¹ 

[1] Department of Biochemistry, Arrhenius Laboratory, University of Stockholm, S-106 91 Stockholm, Sweden

关键词: Glutathione transferase;    4-Hydroxyalk-2-enal;    Detoxication;    Lipid peroxidation;    Glutathione conjugation Reactive metabolite;   

DOI  :  10.1016/0014-5793(86)80743-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rat glutathione transferase 8-8 is one of the less abundant cytosolic glutathione transferases, accounting for approx. 1% of the total activity with 1-chloro-2,4-dinitrobenzene in liver. The enzyme is eluted at pH 6.3 upon chromatofocusing and has so far been identified in liver, kidney, lung and testis. Characteristic properties include high relative activity with ethacrynic acid (70% of the specific activity with 1-chloro-2,4-dinitrobenzene) and an apparent subunit M _r of 24500. The most significant property noted is the high catalytic activity in the conjugation of 4-hydroxyalk-2-enals, major products of lipid peroxidation. The catalytic efficiency with these substrates exceeds corresponding values for all known substrates tested with any glutathione transferase, which suggests that transferase 8-8 may have evolved to detoxify 4-hydroxyalk-2-enals.

【 授权许可】

Unknown