Article
Subspecies of arrestin from bovine retina. Equal functional binding to photoexcited rhodopsin but various isoelectric focusing phenotypes in individuals.
European journal of biochemistry - 24 Oct 1990
Weyand I, Kühn H
Abstract excerpt
Arrestin (also named 48-kDa protein or S-antigen) binds to photoexcited and phosphorylated rhodopsin and thereby prevents activation of cGMP phosphodiesterase (EC 3.1.4.35) by transducin in retinal rods. We report here that retinal arrestin consists of several subspecies (isoelectric points between pH 5.5-6.2), which can be separated by FPLC anion-exchange chromatography and by FPLC chromatofocusing resulting in...
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