CONTRIBUTION OF THE GUANOSINETRIPHOSPHATASE ACTIVITY OF G-PROTEIN TO TERMINATION OF LIGHT-ACTIVATED GUANOSINE CYCLIC 3',5'-PHOSPHATE HYDROLYSIS IN RETINAL ROD OUTER SEGMENTS

被引:27
作者
SITARAMAYYA, A
CASADEVALL, C
BENNETT, N
HAKKI, SI
机构
[1] UNIV PENN,DEPT BIOCHEM,PHILADELPHIA,PA 19104
[2] CEN,BIOPHYS MOLEC & CELLULAIRE LAB,CNRS,UNITE 520,F-38041 GRENOBLE,FRANCE
关键词
D O I
10.1021/bi00413a044
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
引用
收藏
页码:4880 / 4887
页数:8
相关论文
共 59 条
[1]   THE EFFECT OF RHODOPSIN PHOSPHORYLATION ON THE LIGHT-DEPENDENT ACTIVATION OF PHOSPHODIESTERASE FROM BOVINE ROD OUTER SEGMENTS [J].
ARSHAVSKY, VY ;
DIZHOOR, AM ;
SHESTAKOVA, IK ;
PHILIPPOV, PP .
FEBS LETTERS, 1985, 181 (02) :264-266
[2]   ACTIVATION OF ROD OUTER SEGMENT PHOSPHODIESTERASE BY ENZYMATICALLY ALTERED RHODOPSIN - A REGULATORY ROLE FOR THE CARBOXYL TERMINUS OF RHODOPSIN [J].
ATON, B ;
LITMAN, BJ .
EXPERIMENTAL EYE RESEARCH, 1984, 38 (06) :547-559
[3]  
BAEHR W, 1979, J BIOL CHEM, V254, P1669
[4]  
BAEHR W, 1982, J BIOL CHEM, V257, P6452
[5]   THE PHOTOCURRENT, NOISE AND SPECTRAL SENSITIVITY OF RODS OF THE MONKEY MACACA-FASCICULARIS [J].
BAYLOR, DA ;
NUNN, BJ ;
SCHNAPF, JL .
JOURNAL OF PHYSIOLOGY-LONDON, 1984, 357 (DEC) :575-607
[6]   A FUNCTIONAL LINK BETWEEN THE DARK MG-ATPASE ACTIVITY AND THE LIGHT-INDUCED ENZYMATIC CASCADE IN ROD OUTER SEGMENTS [J].
BENNETT, N .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1986, 157 (03) :487-495
[7]  
BENNETT N, 1985, J BIOL CHEM, V260, P4156
[8]   INACTIVATION OF PHOTOEXCITED RHODOPSIN IN RETINAL RODS - THE ROLES OF RHODOPSIN KINASE AND 48-KDA PROTEIN (ARRESTIN) [J].
BENNETT, N ;
SITARAMAYYA, A .
BIOCHEMISTRY, 1988, 27 (05) :1710-1715
[9]   LIGHT-INDUCED INTERACTIONS BETWEEN RHODOPSIN AND THE GTP-BINDING PROTEIN - RELATION WITH PHOSPHODIESTERASE ACTIVATION [J].
BENNETT, N .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1982, 123 (01) :133-139
[10]   PHOSPHORYLATION OF FROG PHOTORECEPTOR MEMBRANES INDUCED BY LIGHT [J].
BOWNDS, D ;
STAHLMAN, M ;
MILLER, J ;
DAWES, J .
NATURE-NEW BIOLOGY, 1972, 237 (73) :125-&