Baumgardner D, Deal C, Kaplan S
J Bacteriol. 1980 Jul;143(1):265-73. doi: 10.1128/jb.143.1.265-273.1980.
The outer membrane polypeptide profile of Rhodopseudmonas sphaeroides was characterized. Solubilization of the outer membrane at 75 or 100 degrees C as opposed to room temperature resulted in the dissociation of 75-, 72-, and 68-kilodalton (kdal) polypeptide aggregates into 29-, 26.5-, and 21.5-kdal polypeptides, respectively, and a shared 47-kdal subunit. Similarly, an 88.5-kdal polypeptide dissociates into a 45-kdal monomeric form, and the electrophoretic mobility of a 58.5-kdal polypeptide was altered to 83 kdal. Lysozyme treatment of outer membrane fractions altered the 21.5-kdal polypeptide mobility to 23 kdal. The presence of lipid in both the 47-kdal polypeptide and an 8- to 10-kdal polypeptide was demonstrated by lipid staining and [14C]acetate incorporation. The lipid component of the 47-kdal polypeptide was neither lipopolysaccharide nor phospholipid. The 8- to 10-kdal polypeptide may be the equivalent of the Braun lipoprotein. Outer membrane fractions isolated from R. sphaeroides-specific phage RS1-resistant mutants were deficient in several of the high-molecular-weight aggregates involving the 47-kdal polypeptide.
对球形红假单胞菌的外膜多肽谱进行了表征。与室温相比,在75或100摄氏度下对外膜进行溶解,导致75、72和68千道尔顿(kdal)的多肽聚集体分别解离为29、26.5和21.5 kdal的多肽,以及一个共享的47 kdal亚基。同样,一个88.5 kdal的多肽解离为45 kdal的单体形式,并且一个58.5 kdal多肽的电泳迁移率改变为83 kdal。对外膜组分进行溶菌酶处理后,21.5 kdal多肽的迁移率改变为23 kdal。通过脂质染色和[14C]乙酸掺入证明了47 kdal多肽和8至10 kdal多肽中均存在脂质。47 kdal多肽的脂质成分既不是脂多糖也不是磷脂。8至10 kdal多肽可能等同于布劳恩脂蛋白。从球形红假单胞菌特异性噬菌体RS1抗性突变体中分离的外膜组分在涉及47 kdal多肽的几种高分子量聚集体中存在缺陷。