Evidence for ATP‐ase activity of arrestin from bovine photoreceptors

FEBS Letters

Glitscher, W.¹  Rüppel, H.¹ 

[1] Max-Volmer-Institute, Technical University Berlin, D-1000 Berlin 12, Germany

关键词: Arrestin;    ATP-hydrolysis;    Rod outer segment;    Signal transduction;    ADP;    adenosine diphosphate;    ATP;    adenosine triphosphate;    cGMP;    cyclic guanosine monophosphate;    DTT;    dithiothreitol;    HEPES;    N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid;    PAGE;    polyacrylamide gel electrophoresis;    PEP;    phosphoenolpyruvate;    PK;    pyruvate kinase;    S;    arrestin;    SDS;    sodium dodecylsulfate;    TCA;    trichloracetic acid;    TEMED;    N;    N;    N;    ′;    N′-tetramethylethene diamine;    Tris;    trishydroxymethyl aminomethane;    ros;    rod outer segment;   

DOI  :  10.1016/0014-5793(91)80530-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown