Evidence for ATP-ase activity of arrestin from bovine photoreceptors.

Abstract:

:In vertebrate photoreceptors the soluble protein arrestin (45 kDa) is involved in controlling the light dependent 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 disease 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 of (5.1 +/- 0.3) x 10(-3) U/mg.min with C1/2 = 93 +/- 5 nM and a Hill coefficient n = 1.8 +/- 0.1 at pH 7.2 and 20 degrees C. These findings suggest a new insight into the process of regulating photoreceptor activity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Glitscher W,Rüppel H

doi

10.1016/0014-5793(91)80530-g

subject

Has Abstract

pub_date

1991-05-06 00:00:00

pages

431-5

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80530-G

journal_volume

282

pub_type

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