LIGHT-INDUCED BINDING OF PROTEINS TO RHABDOMERIC MEMBRANES IN THE RETINA OF CRAYFISH (PROCAMBARUS-CLARKII)

被引：11
作者：
TERAKITA, A
TSUKAHARA, Y
HARIYAMA, T
SEKI, T
TASHIRO, H
机构：
[1] INST CHEM & PHYS RES,PHOTODYNAM RES CTR,PHOTOBIOL LAB,AOBA KU,SENDAI 980,JAPAN
[2] OSAKA KYOIKU UNIV,DEPT HLTH SCI,KASHIWARA 582,JAPAN
[3] TOHOKU UNIV,APPL INFORMAT SCI RES CTR,SENDAI,MIYAGI 980,JAPAN
来源：
VISION RESEARCH | 1993年 / 33卷 / 17期
关键词：
ARRESTIN; G-PROTEIN; RHODOPSIN; RHABDOM; PHOTOTRANSDUCTION; CRAYFISH;
D O I：
10.1016/0042-6989(93)90120-L
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
Light-induced protein interaction as part of the process of visual transduction in arthropods with rhabdomeric photoreceptors was investigated biochemically by using crayfish retina. Two kinds of retinal buffer soluble proteins (one of 40 kDa and the other of 46 kDa) were found to bind to the irradiated rhabdomeric membranes both in vitro and in vivo. The proteins bound to the membranes in the presence of metarhodopsin. An antibody against mouse arrestin (S-antigen) cross-reacted with the 40 kDa protein. These results suggest that the binding of the proteins to the membranes is caused by the formation of metarhodopsin, and that the 40 kDa protein has a similar structure to arrestin.
引用
收藏
页码：2421 / 2426
页数：6
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