Influence of thyroid status on the membranes of rat liver mitochondria Unique localization of L‐glycerol‐3‐phosphate dehydrogenase

FEBS Letters

Beleznai, Z.²  Drahota, Z.¹  Jancsik, V.²  Rauchová, H.¹  Amler, E.¹ 

[1] Institute of Physiology, Czechoslovak Academy of Sciences, Prague, Czechoslovakia;Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary

关键词: Thyroid hormone;    Steady-state fluorescence anisotropy;    Digitonin subfractionation;    FAD-linked L-glycerol-3-phosphate dehydrogenase;    (Rat liver mitochondria;    Mitoplast);    DPH;    diphenylhexa-1;    3;    5-triene;    GDH;    L-glycerol-3-phosphate dehydrogenase;    GluDH;    glutamate dehydrogenase;    MDH;    malate dehydrogenase;    RINCR;    rotenone insensitive NADH-cytochrome-c oxidoreductase;    SDH;    succinate dehydrogenase;    TMA-DPH;    1-[4-{trimethylaminophenyl} phenyl]-6-phenylhexa-1;    3;    5-triene;   

DOI  :  10.1016/0014-5793(89)80138-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of thyroid status on the physical properties of rat liver mitochondrial membranes and on the lipid microenvironment of proteins was investigated. The steady-state fluorescence anisotropy of diphenyl-1,3,5-triene and 1-[4-{trimethylaminophenyl} phenyl]-6-phenylhexa-1,3,5-triene revealed an increase of the order of the membranes with the increase of hormone level. Protein arrangement in the inner mitochondrial membrane altered with the thyroid status, which was reflected by digitonin subfractionation of mitochondria. The microenvironment of FAD-linked L-glycerol-3-phosphate dehydrogenase was dramatically influenced by thyroxine.

【 授权许可】

Unknown