Isoelectric Focusing of Phosphorylated Cattle Rhodopsin

Overview

Journal Biophys Struct Mech

Specialty Biophysics

Date 1977 Jun 29

PMID 890058

Citations 2

Authors

H Kuhn

J H McDowell

Affiliations

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Abstract

32P-rhodopsin was partially separated by isoelectric focusing into several fractions of different phosphorylation extent. It was found that the incorporated phosphate is not uniformly distributed in a population of rhodopsin molecules. In a preparation with an average phosphorylation extent of 2.4 moles of phosphate per mole of rhodopsin, most of the 32P-phosphate was found in fractions where 4-5 phosphates are bound per rhodopsin, whereas a large fraction of the total rhodopsin was not phosphorylated at all. The maximum number os phosphate binding sites in rhodopsin appears to be at least five.

Citing Articles

Effect of Rhodopsin Phosphorylation on Dark Adaptation in Mouse Rods.

Berry J, Frederiksen R, Yao Y, Nymark S, Chen J, Cornwall C J Neurosci. 2016; 36(26):6973-87.

PMID: 27358455 PMC: 4926242. DOI: 10.1523/JNEUROSCI.3544-15.2016.

Rhodopsin phosphorylation occurs at metarhodopsin II level.

Yamamoto K, Shichi H Biophys Struct Mech. 1983; 9(4):259-67.

PMID: 6850048 DOI: 10.1007/BF00535661.

References

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