Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin. | Zendy

Michael Weller | Zendy; N. Virmaux | Zendy; P. Mandel | Zendy

Open Access

Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin.

Author(s) -

Michael Weller,

N. Virmaux,

P. Mandel

Publication year - 1975

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.72.1.381

Subject(s) - rhodopsin , phosvitin , phosphorylation , opsin , biochemistry , protein kinase a , nucleotide , phosphatase , chemistry , enzyme , kinase , histone , biology , dna , retinal , gene

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.

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