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Isoelectric focusing of phosphorylated cattle rhodopsin (1977)

Kühn, Hermann ; McDowell, J. Hugh

Springer

European biophysics journal 3 (1977), S. 199-203

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ISSN: 1432-1017

Keywords: Rhodopsin ; Isoelectric focusing ; Phosphorylation ; Membrane proteins

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Physics

Notes: 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 of phosphate binding sites in rhodopsin appears to be at least five.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00535820

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