视紫红质的光依赖性磷酸化。视紫红质激酶的纯化及性质。 - Suppr

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Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase.

作者信息

Shichi H, Somers R L

出版信息

J Biol Chem. 1978 Oct 10;253(19):7040-6.

PMID:690139

Abstract

摘要

相似文献

Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase.视紫红质的光依赖性磷酸化。视紫红质激酶的纯化及性质。

J Biol Chem. 1978 Oct 10;253(19):7040-6.

Isolation and identification of the phosphorylated species of rhodopsin.视紫红质磷酸化物种的分离与鉴定。

Biochemistry. 1984 Apr 10;23(8):1737-41. doi: 10.1021/bi00303a024.

Light-regulated binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes.视紫红质激酶及其他蛋白质与牛感光细胞膜的光调节结合。

Biochemistry. 1978 Oct 17;17(21):4389-95. doi: 10.1021/bi00614a006.

Characterization of rhodopsin kinase purified from bovine rod outer segments.从牛视杆外段纯化的视紫红质激酶的特性分析。

J Biol Chem. 1990 Feb 15;265(5):2632-9.

Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin.视网膜中视紫红质的光刺激磷酸化：存在一种对视紫红质光漂白具有特异性的蛋白激酶。

Proc Natl Acad Sci U S A. 1975 Jan;72(1):381-5. doi: 10.1073/pnas.72.1.381.

Phosphorylation of rhodopsin and quenching of cyclic GMP phosphodiesterase activation by ATP at weak bleaches.在弱漂白条件下视紫红质的磷酸化以及ATP对环鸟苷酸磷酸二酯酶激活的淬灭作用。

J Biol Chem. 1983 Oct 25;258(20):12106-9.

Rhodopsin phosphorylation occurs at metarhodopsin II level.视紫红质磷酸化发生在变视紫红质II水平。

Biophys Struct Mech. 1983;9(4):259-67. doi: 10.1007/BF00535661.

Protein kinases of retinal rod outer segments: identification and partial characterization of cyclic nucleotide dependent protein kinase and rhodopsin kinase.视网膜视杆细胞外段的蛋白激酶：环核苷酸依赖性蛋白激酶和视紫红质激酶的鉴定及部分特性研究

Biochemistry. 1981 Dec 22;20(26):7532-8. doi: 10.1021/bi00529a031.

Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.席夫碱去质子化对于光依赖性视紫红质磷酸化是必需的。

Biochem J. 1989 Dec 1;264(2):489-93. doi: 10.1042/bj2640489.

Purification and characterization of rhodopsin kinase.视紫红质激酶的纯化与特性分析

J Biol Chem. 1988 Oct 5;263(28):14067-73.

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