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Evidence for ATP‐ase activity of arrestin from bovine photoreceptors
Author(s) -
Glitscher W.,
Rüppel H.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80530-g
Subject(s) - arrestin , transducin , phosphodiesterase , receptor , microbiology and biotechnology , retinal , chemistry , biology , rhodopsin , biophysics , biochemistry , enzyme , g protein coupled receptor
In vertebrate photoreceptors the soluble protein arrestin (45 kDa) is involved in controlling the light dependence activity of receptor proteins such as transducin or the cGMP‐phosphodiesterase. Arrestin has further been identified as the retinal‐S‐antigen which is assumed to cause the autoimmune discase uveitis. In a first communication a binding of the nucleotide ATP to arrestin was described. In this subsequent study it is shown that arrestin is also able to hydrolyse ATP at a rate (5.1 ±0.3)·10 −3 U/mg min with C = 93±5 nM and a Hill coefficient n = 1.8±0.1 at pH 7.2 and 20°C. These findings suggest a new insight into the process of regulating photoreceptor activity.