An arrestin homolog of blowfly photoreceptors stimulates visual‐pigment phosphorylation by activating a membrane‐associated protein kinase

An arrestin homolog (Arr2, 49‐kDa protein) of blowfly (Calliphora erythrocephala) retinae undergoes light‐dependent reversible binding to the photoreceptor membrane. In order to characterize this arrestin homolog and to study its function in a well‐defined experimental system, we developed a purific...

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Veröffentlicht in:	European journal of biochemistry 1993-08, Vol.216 (1), p.67-73
Hauptverfasser:	BENTROP, Joachim, PLANGGER, Anette, PAULSEN, Reinhard
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Arrestins Binding Sites Calliphora erythrocephala Calliphoridae Cell Membrane - enzymology Diptera Electrophoresis, Polyacrylamide Gel Enzyme Activation Eye Proteins - chemistry Eye Proteins - isolation & purification Eye Proteins - metabolism G-Protein-Coupled Receptor Kinase 1 Isoelectric Focusing Light Microvilli - metabolism Phosphoproteins - chemistry Phosphoproteins - isolation & purification Phosphoproteins - metabolism Phosphorylation Photoreceptor Cells - metabolism Protein Kinases - chemistry Protein Kinases - metabolism Rhodopsin - metabolism Urea - pharmacology
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