Knowles A, Pepe I M
Department of Biochemistry, University of Bristol, England.
Cell Biophys. 1988 Aug;13(1):43-53. doi: 10.1007/BF02797364.
The rod photoreceptors of vertebrate retinas contain a cGMP phosphodiesterase (PDE) that is activated by light. The light is absorbed by rhodopsin that activates an intermediate GTP-binding protein; this species then activates the PDE. Photo-excited rhodopsin passes through a series of transient states, and the purpose of this study is to identify the earliest state that interacts with the GTP-binding protein and thus activate the PDE. The majority of evidence points to this state being metarhodopsin II (MII), but PDE activation is seen at low temperatures where the rhodopsin reaction sequence is not expected to pass beyond the metarhodopsin I (MI) stage. Light thresholds for PDE activation have been determined under conditions where little MII is generated, and these are compared with the concentration of MII. The conclusion is that for a criterion threshold of PDE activity, the MII concentration is constant, irrespective of the amount of MI present, which suggests that MI cannot activate the PDE system.
脊椎动物视网膜的视杆光感受器含有一种受光激活的环鸟苷酸磷酸二酯酶(PDE)。光被视紫红质吸收,视紫红质激活一种中间GTP结合蛋白;该蛋白随后激活PDE。光激发的视紫红质会经历一系列瞬态,本研究的目的是确定与GTP结合蛋白相互作用并因此激活PDE的最早状态。大多数证据表明这种状态是变视紫红质II(MII),但在低温下也能观察到PDE激活,而在低温下视紫红质反应序列预计不会超过变视紫红质I(MI)阶段。在几乎不产生MII的条件下确定了PDE激活的光阈值,并将其与MII的浓度进行比较。结论是,对于PDE活性的标准阈值,MII浓度是恒定的,与存在的MI量无关,这表明MI不能激活PDE系统。