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The study aims to purify rhodopsin kinase and explore its properties, specifically regarding light-dependent phosphorylation of rhodopsin.

Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase.

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The study aims to purify rhodopsin kinase and explore its properties, specifically regarding light-dependent phosphorylation of rhodopsin.
Rhodopsin kinase was extracted from bovine rod outer segments using 1 M ammonium chloride and purified through ammonium sulfate fractionation and chromatography.
Characterization included polyacrylamide gel electrophoresis for evaluating homogeneity and estimating molecular weight.
Phosphorylation assays were conducted to determine substrate specificity and inhibition by various ions and nucleotides.
Rhodopsin kinase had a molecular weight of 50,000 to 53,000 with no evidence of subunit composition.
Phosphate incorporation was found to be about 16% of total pigment, indicating multiphosphorylation sites in a fraction of rhodopsin.
Phosphorylated pigment showed higher radioactivity in newly formed discs compared to unphosphorylated pigment, suggesting localization of phosphorylation within the plasma membrane.

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Randomized trial investigates phosphorylation of rhodopsin by rhodopsin kinase, highlighting enzyme specificity and cellular location.

Shichi et al. (1978) studied this question.

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