Abstract
A protein kinase has been extracted from bovine rod outer segments by a mild procedure. The enzyme acts specifically on photobleached, not unbleached, rhodopsin and will not catalyze the phosphorylation of histones, phosvitin, or casein. We propose the name "opsin kinase" for the enzyme, which is not affected by cyclic nucleotides but which is inhibited by theophylline. Preparations of purified rod outer segments, however, appear to contain only low concentration of opsin phosphatase activity.
MeSH Terms
Adenosine Triphosphate/metabolism
Animals
Caseins/metabolism
Cattle
Cyclic AMP/pharmacology
Cyclic GMP/pharmacology
Enzyme Activation/drug effects
Histones/metabolism
Light
Phosphates/metabolism
Phosphodiesterase Inhibitors
Phosphorus Radioisotopes
Photic Stimulation
Photoreceptor Cells/enzymology,metabolism
Protein Kinases/metabolism
Retinal Pigments/metabolism
Rhodopsin/metabolism
Theophylline/pharmacology
Chemicals
Caseins
Histones
Phosphates
Phosphodiesterase Inhibitors
Phosphorus Radioisotopes
Retinal Pigments
Adenosine Triphosphate
Rhodopsin
Theophylline
Cyclic AMP
Protein Kinases
Cyclic GMP
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Weller M
Virmaux N
Mandel P
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25 references, click to expand
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