Højrup P, Gerola P, Hansen H F, Mikkelsen J M, Shahed A E, Knudsen J, Roepstorff P, Olson J M
Department of Molecular Biology, Odense University, Denmark.
Biochim Biophys Acta. 1991 Apr 8;1077(2):220-4. doi: 10.1016/0167-4838(91)90061-4.
A 7.5-kDa protein has been isolated from chlorosomes of Chlorobium limicola f. thiosulfatophilum and the complete primary structure determined by a combination of automatic Edman degradation and plasma desorption mass spectrometry. The 74-residue protein shows great homology to a similar protein of unknown function which has been isolated from Pelodictyon luteolum but otherwise no significant homology to other proteins can be found. The possible role of the protein in the structure and function of the chlorosome is discussed.
一种7.5千道尔顿的蛋白质已从嗜硫代硫酸盐绿弯菌的叶绿体中分离出来，并通过自动埃德曼降解和等离子体解吸质谱联用确定了其完整的一级结构。这种由74个氨基酸残基组成的蛋白质与从黄皮生绿菌中分离出的一种功能未知的类似蛋白质具有高度同源性，但与其他蛋白质没有明显的同源性。本文讨论了该蛋白质在叶绿体结构和功能中的可能作用。
