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Similarities between G‐proteins in visual cells of Sepia and cattle
Author(s) -
Stieve Hennig,
Lumme Gisela
Publication year - 1989
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(89)80918-4
Subject(s) - transducin , sepia , rhodopsin , antiserum , cuttlefish , gtp' , polyclonal antibodies , g protein , visual phototransduction , biochemistry , biology , chemistry , antibody , retinal , officinalis , enzyme , receptor , botany , fishery , immunology
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.