Similarities between G‐proteins in visual cells of Sepia and cattle

FEBS Letters

Lumme, Gisela¹  Stieve, Hennig¹ 

[1] Institut für Biologie II (Zoologie) RWTH Aachen, Kopernikusstr. 16,5100 Aachen, FRG

关键词: Visual transduction;    G-protein;    Heat denaturation;    Antibody;    Crossreaction;    (Sepia officinalis);    PLC;    phospholipase C;    GTP;    guanosine trisphosphate;    GDP;    guanosine diphosphate;    G-protein;    GTP-binding protein;    Tα;    Tβγ;    subunits of transducin (G-protein of vertebrate photoreceptor);    Gα;    Gβ;    subunits of G-protein;    cGMP;    cyclic guanosine monophosphate;    DTT;    dithiothreitol;    Hepes;    N-(2-hydroxyethyl)piperazine N′-2-ethanesulfonic acid;    PMSF;    phenylmethylsulfonyl fluoride;    Tris;    tris(hydroxymethyl) aminomethane;   

DOI  :  10.1016/0014-5793(89)80918-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In contrast to antisera against native transducin a polyclonal antiserum raised against heat-denatured bovine transducin crossreacts with the G-protein from Sepia visual cells. This antiserum recognizes a 44 kDa (G_α) and a 36 kDa (G_β) protein band from Sepia photosensory membrane preparation. Furthermore we purified the antibody-binding G-protein from Sepia by binding it to light-activated rhodopsin of Sepia and GTP-induced extraction, similar to the purification of bovine transducin. This G-protein is probably involved in the phototransduction process. The purified Sepia G-protein did bind to vertebrate photosensoric membrane upon illumination, but was not eluted by GTP-containing buffer solution. After extensive bleaching, the G-protein became soluble.

【 授权许可】

Unknown