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  • Phosphorylation  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 3 (1977), S. 175-180 
    ISSN: 1432-1017
    Keywords: Rodopsin ; Phosphorylation ; Adaptation ; Retina ; Cyclic nucleotides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Light-induced phosphorylation of rhodopsin has been extensively studied by a number of investigators from a biochemical point of view. However, little is known about the physiological function of this reaction. The slow rates measured for phosphorylation and dephosphorylation suggest that it may be involved in visual adaptation rather than in excitation. This paper presents biochemical data obtained from phosphorylation experiments in isolated photoreceptor membranes as well as in the more physiological system of whole retinas and living animals. An attempt is made to compare the phosphorylation reaction with visual adaptation hypotheses taken from the electrophysiological literature. Finally, effects of cyclic nucleotide metabolism on the sensitivity of photoreceptors are presented and discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 3 (1977), S. 199-203 
    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
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