Institut für Mikrobiologie der Georg-August-Universität Göttingen, Grisebachstrasse 8, D-3400 Göttingen, Federal Republic of Germany.
Proc Natl Acad Sci U S A. 1986 Aug;83(16):5789-92. doi: 10.1073/pnas.83.16.5789.
Antibodies were raised against homogeneous preparations of component C of the methylreductase system from Methanococcus voltae and Methanobacterium thermoautotrophicum. Cells of these organisms were fixed with paraformaldehyde and/or glutaraldehyde, sectioned, and labeled with antibodies and colloidal gold-labeled protein A. In M. voltae the gold particles were predominantly located in the vicinity of the cytoplasmic membrane. In rare cases a similar result was obtained also with M. thermoautotrophicum. However, in all but a few of the ultrathin sections of this bacterium, the label was randomly distributed in the cell interior. If one assumes a reliable fixation of all cell components, these results would suggest that the two distantly related methanogens studied have distinctive patterns for the localization of component C. The results with M. voltae are in agreement with recent findings that the methylreductase system is involved in the generation of a proton-motive force at the membrane.
针对来自 Methanococcus voltae 和 Methanobacterium thermoautotrophicum 的甲基还原酶系统成分 C 的均相制剂,制备了抗体。用多聚甲醛和/或戊二醛固定这些生物体的细胞,切片,并用抗体和胶体金标记的蛋白 A 进行标记。在 M. voltae 中,金颗粒主要位于细胞质膜附近。在极少数情况下,也可以从 M. thermoautotrophicum 中获得类似的结果。然而,在除了这种细菌的少数几个超薄切片之外,标记随机分布在细胞内部。如果假定所有细胞成分都得到了可靠的固定,那么这些结果表明,研究的两种亲缘关系较远的产甲烷菌在成分 C 的定位上具有独特的模式。与最近的发现一致,M. voltae 的结果表明,甲基还原酶系统参与在膜上产生质子动力。