Department of Chemistry, University of Crete, Iraklion, Crete, Greece.
Photosynth Res. 1994 Oct;42(1):37-42. doi: 10.1007/BF00019056.
A highly purified oxygen evolving Photosystem II core complex was isolated from PS II membranes solubilized with the non-ionic detergent n-octyl-β-D-thioglucoside. The three extrinsic proteins (33, 23 and 17 kDa) were functionally bound to the PS II core complex. Selective extraction of the 22, 10 kDa, CP 26 and CP 29 proteins demonstrated that these species are not involved in the binding of the extrinsic proteins (33, 23 and 17 kDa) or the DCMU sensitivity of the Photosystem II complex.
从用非离子型去污剂 n-辛基-β-D-硫代吡喃葡萄糖苷溶解的 PS II 膜中分离出高度纯化的产氧光合系统 II 核心复合物。三种外在蛋白(33、23 和 17 kDa)与 PS II 核心复合物有功能结合。选择性提取 22、10 kDa、CP 26 和 CP 29 蛋白表明,这些物质不参与外在蛋白(33、23 和 17 kDa)的结合或 PS II 复合物对 DCMU 的敏感性。