Jacob J S, Miller K R
Arch Biochem Biophys. 1983 May;223(1):282-90. doi: 10.1016/0003-9861(83)90593-3.
A procedure for the isolation of highly purified bacterial photosynthetic membranes from Rhodopseudomonas viridis is described. The purity of the final membrane fraction has been confirmed by electron microscopy. Seven major polypeptide bands are associated with the photosynthetic membranes, and all seven are resistant to solubilization in Triton X-100 detergent. Two pigmented bands with apparent molecular weights of 44K and 41K are thought to be cytochromes. The three polypeptides with apparent molecular weights of 38K, 32K, and 28K have been reported in reaction center preparations of other laboratories. Two low-molecular-weight (16K and 11K) bands bind bacteriochlorophyll b and may represent light-harvesting bacteriochlorophyll-protein complexes. The structures that were isolated seem to represent complete photosynthetic membranes, consisting of reaction center, electron transport, and light-harvesting components, all arranged in the regular lattice characteristic of viridis. Selective proteolysis of these membranes indicates that all membrane components are accessible to digestion by trypsin and pronase, except for the light-harvesting complexes.
本文描述了一种从绿色红假单胞菌中分离高纯度细菌光合膜的方法。最终膜组分的纯度已通过电子显微镜确认。七条主要的多肽带与光合膜相关，并且所有七条都对Triton X - 100去污剂的溶解具有抗性。两条表观分子量为44K和41K的色素带被认为是细胞色素。其他实验室在反应中心制剂中已报道了表观分子量为38K、32K和28K的三种多肽。两条低分子量（16K和11K）的带结合细菌叶绿素b，可能代表捕光细菌叶绿素 - 蛋白质复合物。分离得到的结构似乎代表完整的光合膜，由反应中心、电子传递和捕光组分组成，所有这些都以绿色红假单胞菌特有的规则晶格排列。对这些膜的选择性蛋白酶解表明，除了捕光复合物外，所有膜组分都可被胰蛋白酶和链霉蛋白酶消化。
