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Purification method of bovine rhodopsin kinase using regeneration of rhodopsin

โœ Scribed by Daisuke Okada; Atsushi Ikai

Publisher
Elsevier Science
Year
1988
Tongue
English
Weight
430 KB
Volume
169
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

We report a rapid and high-yield purification method of bovine retinal rhodopsin kinase. According to our method, 500 micrograms of rhodopsin kinase was purified from 100 bovine retinae within 12 h. Rhodopsin kinase bound to bleached rhodopsin was extracted effectively from rod outer segment membranes after regeneration of rhodopsin by the incubation with exogenous 11-cis-retinal. Subsequent DE52 column chromatography further purified the protein to homogeneity on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified rhodopsin kinase had an apparent molecular weight of 68,000 and phosphorylated rhodopsin at the rate of 10 nmol phosphate/min/mg of the enzyme.

๐Ÿ“œ SIMILAR VOLUMES

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โœ Satoshi Hara; Edward L. Kean ๐Ÿ“‚ Article ๐Ÿ“… 1983 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 372 KB

The molecular weight of a glycopeptide cleaved enzymatically from bovine rhodopsin was investigated by a variety of techniques, such as gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence and absence of urea, and gel filtration in 6 M guanidinium chloride after