Angus B L, Hancock R E
J Bacteriol. 1983 Sep;155(3):1042-51. doi: 10.1128/jb.155.3.1042-1051.1983.
Native oligomers of three Pseudomonas aeruginosa outer membrane porin proteins and one Escherichia coli porin were demonstrated by using a chemical cross-linking technique. P. aeruginosa protein F, the major constitutive outer membrane porin, was cross-linked to dimers in outer membrane and whole-cell cross-linking experiments. Purified preparations of P. aeruginosa proteins F, D1 (glucose induced), and P (phosphate starvation induced) and E. coli protein PhoE (Ic) were also cross-linked to reveal dimers and trimers upon two-dimensional sodium dodecyl sulfate-polyacrylamide electrophoretic analysis. Cross-linking of protein F was abolished by pretreatment of the protein with sodium dodecyl sulfate, indicating that the cross-linked products were due to native associations in the outer membrane.
利用化学交联技术证实了三种铜绿假单胞菌外膜孔蛋白和一种大肠杆菌孔蛋白的天然寡聚体。铜绿假单胞菌蛋白F是主要的组成型外膜孔蛋白，在细胞膜和全细胞交联实验中被交联成二聚体。纯化的铜绿假单胞菌蛋白F、D1（葡萄糖诱导型）、P（磷酸盐饥饿诱导型）和大肠杆菌蛋白PhoE（Ic）也进行了交联，通过二维十二烷基硫酸钠-聚丙烯酰胺电泳分析发现了二聚体和三聚体。用十二烷基硫酸钠预处理蛋白F后，其交联作用消失，这表明交联产物是由于外膜中的天然缔合作用。
