A Ca2+-Binding Protein that Regulates the Lifetime of the Transducin Active State

被引：0

作者：

Petrukhin O.V. ^{[1
]}

Orlova T.G. ^{[1
]}

Nezvetsky A.R. ^{[1
]}

Orlov N.Y. ^{[1
]}

机构：

[1] Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290, Moscow oblast

来源：

Biophysics | 2019年 / 64卷 / 5期

关键词：

affinity chromatography; Ca[!sup]2+[!/sup]-binding proteins of retinal photoreceptors; calmodulin-sepharose; G-proteins; GMP-specific phosphodiesterase; Keywords: retinal rod outer segments; regulation with Mg[!sup]2+[!/sup] and Ca[!sup]2+[!/sup] ions; system of phototransduction; transducin;

D O I：

10.1134/S0006350919050208

中图分类号：

学科分类号：

摘要：

Abstract—It has been previously shown in the study of the kinetic behavior of cGMP-specific phosphodiesterase in preparations of the outer segments of bovine retinal rods, which was temporarily activated by 2 μM GTP at high and low concentrations of free ions of Ca2+ (100 μM and <10 nm, respectively), that the lifetime of cGMP-specific phosphodiesterase in the active state significantly decreased (by ≈2 times) when low concentrations of free calcium ions were used. This suggested that there is a Ca2+-binding protein in the outer segments of bovine retinal rods that can interact with the so-called free transducin and regulate the rate of hydrolysis of GTP, which is bound in its active site, depending on the concentration of free Ca2+ ions. This paper is devoted to a discussion of the known Ca2+-binding proteins that occur in the outer segments of bovine retinal rods that could play the role of a potential regulator. © 2019, Pleiades Publishing, Inc.

引用

页码：694 / 695

页数：1

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