PMID: 6986913Feb 28, 1980Paper

Protein neighborhoods in the outer membrane of Salmonella typhimurium

Biochimica Et Biophysica Acta
E T Palva

Abstract

The organization of proteins in the outer membrane of Salmonella typhimurium was analyzed by cross-linking with cleavable reagents and symmetrical two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis. The major outer membrane proteins could be cross-linked to form multimeric complexes. The pore-forming 44 000, 36 000 and 34 000 dalton proteins were cross-linked to form dimers and trimers. Lipoprotein was cross-linked to 33 000 and 17 500 dalton proteins. In addition the 33 000, 24 000, 17 500 dalton proteins and the free form of lipoprotein were cross-linked to the peptidoglycan layer of the cell wall. The cross-linked complexes found were similar to those of analogous proteins in the outer membrane of Escherichia coli, thus suggesting a similar organization of outer membrane proteins in these species.

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Citations

Jan 1, 1986·Critical Reviews in Microbiology·T Nakae
Aug 9, 2018·Proceedings of the National Academy of Sciences of the United States of America·Matthew J Powers, M Stephen Trent
Aug 20, 2019·The Journal of Biological Chemistry·Rahul Shrivastava, Shu-Sin Chng
Jan 22, 2015·Antimicrobial Agents and Chemotherapy·Erica J RubinM Stephen Trent

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