Zürrer H, Snozzi M, Hanselmann K, Bachofen R
Biochim Biophys Acta. 1977 May 11;460(2):273-9. doi: 10.1016/0005-2728(77)90213-4.
Reaction centers were isolated with the detergent lauryl dimethyl amine oxide from chromatophore membranes of Rhodospirillum rubrum. The subunit composition of these reaction centers is similar to the one obtained from Rhodopseudomonas spheroides: three subunits with the molecular weights of 21 000, 24 000 and 29 000. Reaction centers prepared from chromatophores labeled with 131I were heavely labeled in their large subunit (H). The smaller subunits (L and M) contained only little label. Sonication during labeling yielded a slightly higher incorporation of 131I in subunit H compared to the smaller ones. It is concluded that the H protein is largely exposed at the cytoplasmic side of the membrane but might also be accessible for iodination on the inside of the membrane while the L and M proteins are almost completely embedded in the membrane. Iodination of spheroplasts results in only a slight binding of 131I to chromatophores and reaction centers.
用去污剂月桂基二甲基氧化胺从深红红螺菌的载色体膜中分离出反应中心。这些反应中心的亚基组成与从球形红假单胞菌获得的相似:三个亚基的分子量分别为21000、24000和29000。用131I标记的载色体制备的反应中心在其大亚基(H)中被大量标记。较小的亚基(L和M)仅含有少量标记。与较小亚基相比,标记过程中的超声处理使131I在亚基H中的掺入量略高。得出的结论是,H蛋白在很大程度上暴露于膜的细胞质侧,但在膜内部也可能易于碘化,而L和M蛋白几乎完全嵌入膜中。原生质球的碘化仅导致131I与载色体和反应中心的轻微结合。