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Of the 17 strains examined, 12 expressed a phosphate-starvation-induced outer membrane protein which was heat modifiable in that after solubilization in sodium dodecyl sulfate at low temperature the protein ran on gels as a diffuse band of higher apparent molecular weight, presumably an oligomer form, which shifted to an apparent monomer form after solubilization at high temperature. These proteins fell into two classes based on their monomer molecular weights and the detergent conditions required to release the proteins from the peptidoglycan. The first class, expressed by species of the Pseudomonas fluorescens branch of the family Pseudomonadaceae, was similar to the phosphate-starvation-inducible, channel-forming protein P of Pseudomonas aeruginosa. The second class resembled the major enterobacterial porin proteins and the phosphate-regulated PhoE protein of Escherichia coli. Using a protein P-trimer-specific polyclonal antiserum, we were able to demonstrate cross-reactivity of the oligomeric forms of both classes of these proteins on Western blots. However, this antiserum did not react with the monomeric forms of any of these proteins, including protein P monomers. With a protein P-monomer-specific antiserum, no reactivity was seen with any of the phosphate-starvation-inducible membrane proteins (in either oligomeric or monomeric form), with the exception of protein P monomers. These results suggest the presence of conserved antigenic determinants only in the native, functional proteins.<\/jats:p>","DOI":"10.1128\/jb.165.3.987-993.1986","type":"journal-article","created":{"date-parts":[[2016,11,2]],"date-time":"2016-11-02T21:28:31Z","timestamp":1478122111000},"page":"987-993","update-policy":"http:\/\/dx.doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":42,"title":["Phosphate-starvation-induced outer membrane proteins of members of the families Enterobacteriaceae and Pseudomonodaceae: demonstration of immunological cross-reactivity with an antiserum specific for porin protein P of Pseudomonas aeruginosa"],"prefix":"10.1128","volume":"165","author":[{"given":"K","family":"Poole","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R E","family":"Hancock","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"p_1","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1128\/jb.155.3.1042-1051.1983","article-title":"Outer membrane porin proteins F, P, and Dl of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers","volume":"155","author":"Angus B. 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Bacteriol."},{"key":"p_3","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1111\/j.1432-1033.1984.tb08104.x","article-title":"Outer membrane protein PhoE from Escherichia coli forms anionselective pores in lipid bilayer membranes","volume":"140","author":"Benz R.","year":"1984","unstructured":"Benz , R. , RF P . Darveau , and R. E. W. Hancock . 1984 . Outer membrane protein PhoE from Escherichia coli forms anionselective pores in lipid bilayer membranes . Eur. J. Biochem. 140 : 319 - 324 .","journal-title":"Eur. J. Biochem."},{"key":"p_4","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1128\/jb.162.2.722-727.1985","article-title":"Ion selectivity of gram-negative bacterial porin","volume":"162","author":"Benz R.","year":"1985","unstructured":"Benz , R. , A. Schmid , and R. E. W. Hancock . 1985 . Ion selectivity of gram-negative bacterial porin . J. Bacteriol. 162 : 722 - 727 .","journal-title":"J. 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B.","year":"1976","unstructured":"Russell , R. R. B. 1976 . Two-dimensional SDS-polyacrylamide gel electrophoresis of heat-modifiable outer-membrane proteins . Can. J. Microbiol. 22 : 83 - 91 .","journal-title":"Can. J. Microbiol."},{"key":"p_26","first-page":"2347","article-title":"Influence of nutrient limitation and growth rate on the outer membrane proteins of Klebsiella aerogenes NCTC 418","volume":"130","author":"Sterkenburg A.","year":"1984","unstructured":"Sterkenburg , A. , E. Viegels , and J. T. M. Wouters . 1984 . Influence of nutrient limitation and growth rate on the outer membrane proteins of Klebsiella aerogenes NCTC 418 . J. Gen. Microbiol. 130 : 2347 - 2355 .","journal-title":"J. Gen. Microbiol."},{"key":"p_27","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1128\/jb.139.2.376-383.1979","article-title":"Mutants defective in the 33K outer membrane protein of Salmonella typhimurium","volume":"139","author":"Stocker B. A. 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