Wagner-Huber R, Fischer U, Brunisholz R, Rümbeli M, Frank G, Zuber H
Institut für Molekularbiologie und Biophysik, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.
Z Naturforsch C J Biosci. 1990 Jul-Aug;45(7-8):818-22. doi: 10.1515/znc-1990-7-812.
In addition to the previous isolated and sequenced polypeptides from green photosynthetic sulfur bacteria, which are presumably involved in binding BChl c and e, an analogous polypeptide has been purified from the BChl d-containing bacterium Chlorobium vibrioforme f. thiosulfatophilum. The primary structure of this 6.15 kDa polypeptide was determined. It shows an extremely high homology (98.3%) to the corresponding polypeptide from Pelodictyon luteolum, indicative of an important functional role.
除了之前从绿色光合硫细菌中分离并测序的可能参与结合叶绿素c和e的多肽外，还从含有叶绿素d的硫代硫酸盐嗜绿菌（Chlorobium vibrioforme f. thiosulfatophilum）中纯化出了一种类似的多肽。确定了这种6.15 kDa多肽的一级结构。它与来自黄斑绿菌（Pelodictyon luteolum）的相应多肽显示出极高的同源性（98.3%），表明其具有重要的功能作用。
