CHICKEN RED-SENSITIVE CONE VISUAL PIGMENT RETAINS A BINDING DOMAIN FOR TRANSDUCIN

CHICKEN RED-SENSITIVE CONE VISUAL PIGMENT RETAINS A BINDING DOMAIN FOR TRANSDUCIN
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DOI:
10.1016/0014-5793(89)80255-8
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发表时间:
1989-03-27
期刊:
影响因子:
3.5
通讯作者:
YOSHIZAWA, T
YOSHIZAWA, T
中科院分区:
生物学3区
文献类型:
--
作者:
FUKADA, Y;OKANO, T;YOSHIZAWA, T

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从鸡视网膜中分离出碘视蛋白(一种红色敏感的视锥细胞色素)和视紫红质(一种视杆细胞色素)。将它们分别重组到磷脂酰胆碱脂质体中,然后与从牛视网膜中纯化的视杆细胞转导素(Tα和Tβγ)混合。碘视蛋白仅在照射时增强GppNHp与Tα的结合,其程度与照射后的视紫红质相似。此外,在碘视蛋白的光漂白中间体的存在下,GppNHp与Tα的结合优选地需要Tβγ-2而不是Tβγ-1,这与视紫红质的中间体的存在下的特征非常相似(J. Biol. Chem.,印刷中)。这些结果表明,在碘视蛋白转导的结合域应该非常类似于在视紫红质。
Iodopsin (a red‐sensitive cone visual pigment) and rhodopsin (a rod pigment) were isolated from chicken retina. They were separately reconstituted into phosphatidylcholine liposomes and then mixed with rod transducin (Tα and Tβγ) purified from bovine retina. Iodopsin enhanced, only when irradiated, the binding of GppNHp to Tα to a similar extent to irradiated rhodopsin. Furthermore, the binding of GppNHp to Tα in the presence of a photobleaching intermediate of iodopsin preferably required Tβγ‐2 rather than Tβγ‐1, which is very similar in profile to that in the presence of the intermediate of rhodopsin (J. Biol. Chem., in press). These results indicate that the binding domain for transducin in iodopsin should closely resemble that in rhodopsin.