Poggese C, Polverino de Laureto P, Giacometti G M, Rigoni F, Barbato R
Dipartimento di Biologia, Università di Padova, Padua, Italy.
FEBS Lett. 1997 Sep 15;414(3):585-9. doi: 10.1016/s0014-5793(97)01078-8.
Fractionation of photosynthetic membranes from the cyanobacterium Synechocystis 6803 by polyacrylamide gel electrophoresis in the presence of Deriphat-160 allowed the isolation of a number of pigmented bands. Two of them, with molecular masses of 240+/-20 and 110+/-15 kDa respectively, showed peroxidase activity and, by means of polypeptide composition, immunoblotting and N-terminal sequencing, were identified as dimeric and monomeric cytochrome b6/f complexes, containing 1.3+/-0.35 chlorophyll molecules per cytochrome f. Further fractionation of monomeric complexes by mild gel electrophoresis in the presence of sodium dodecyl sulfate indicated that it is the cytochrome b6 polypeptide which provides the actual binding site for the chlorophyll molecule observed in the complex.
在存在Deriphat-160的情况下,通过聚丙烯酰胺凝胶电泳对蓝藻集胞藻6803的光合膜进行分级分离,得以分离出多个色素条带。其中两条带,分子量分别为240±20 kDa和110±15 kDa,显示出过氧化物酶活性,并且通过多肽组成、免疫印迹和N端测序,被鉴定为二聚体和单体细胞色素b6/f复合物,每个细胞色素f含有1.3±0.35个叶绿素分子。在十二烷基硫酸钠存在的情况下,通过温和的凝胶电泳对单体复合物进行进一步分级分离表明,正是细胞色素b6多肽为复合物中观察到的叶绿素分子提供了实际的结合位点。