Characterization of a spinach photosystem II core preparation isolated by a simplified method
A photosystem II core complex from spinach exhibiting high rates of electron transport was obtained rapidly and in high yield by treatment of a Tris-extracted, O2-evolving photosystem II preparation with the detergent dodecyl-β-d-maltoside. The core complex was essentially free of light-harvesting chlorophyll-protein and photosystem I polypeptides, and was highly enriched in the polypeptides associated with the photosystem II reaction center (45 and 49 kDa), cytochrome b559, and three polypeptides in the region 32-34 kDa. The photosystem II core complex contained two chlorophyll-proteins which had a slightly higher apparent molecular mass than CPa-1 and CPa-2. Additionally, a high-molecular-mass chlorophyll-protein complex termed CPa* was observed, which exhibited a low fluorescence yield when illuminated with ultraviolet light. This observation suggests that CPa* contains a functionally efficient quencher of chlorophyll fluorescence, possibly P680. © 1985.
Publication Source (Journal or Book title)
Archives of Biochemistry and Biophysics
Bricker, T., Pakrasi, H., & Sherman, L. (1985). Characterization of a spinach photosystem II core preparation isolated by a simplified method. Archives of Biochemistry and Biophysics, 237 (1), 170-176. https://doi.org/10.1016/0003-9861(85)90266-8