Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers
- 1 September 1983
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 155 (3) , 1042-1051
- https://doi.org/10.1128/jb.155.3.1042-1051.1983
Abstract
Native oligomers of 3 P. aeruginosa outer membrane porin proteins and 1 E. 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 were also cross-linked to reveal dimers and trimers upon 2-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.This publication has 36 references indexed in Scilit:
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