Isolation and Characterization of Lipopolysaccharide Protein from
            <i>Escherichia coli</i>

Wu, Ming‐Chi; Heath, Edward C.

doi:10.1073/pnas.70.9.2572

Cited by 41 publications

(19 citation statements)

References 19 publications

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“…The apparent molecular weights of the two major outer membrane proteins that are preferentially synthesized upon the onset of leucine deprivation are 32,000 4,000 and 13,000 + 2,000 as determined from the average of several separations on SDS-polyacrylamide gels. The molecular weights of these two protein frac- tions correspond fairly well to those of envelope proteins studied previously by Rosenbusch (21) and by Wu and Heath (29). The protein characterized by Rosenbusch is the major E. coli envelope protein, having a molecular weight on SDS-polyacrylamide gel electrophoresis of 36,500 and comprising about 7% of the total cellular protein.…”

Section: Resultssupporting

confidence: 82%

Protein synthesis and degradation in a leucine auxotroph of Escherichia coli

Aguanno¹,

Larrabee²

1976

J Bacteriol

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The synthesis and degradation of the soluble and sodium dodecyl sulfate-(SDS)-solubilized protein fractions of Escherichia coli were studied in both growing and nongrowing cultures. When separated according to molecular weight on SDS-polyacrylamide gels, the proteins of both fractions of growing cells undergo no measureable differential synthesis or degradation during logarithmic growth. However, when a leucine auxotroph is suspended in medium containing 5.3 muM leucine (a level that will not sustain growth), the SDS-solubilized protein of such a nongrowing culture shows a rapid synthesis of two protein components (32,000 and 12,000 daltons) found only in the out membrane.

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Section: Resultssupporting

confidence: 82%

Protein synthesis and degradation in a leucine auxotroph of Escherichia coli

Aguanno¹,

Larrabee²

1976

J Bacteriol

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“…Since all LPSs used were extracted by the hot phenol-water method, our results obtained for mitogenic activity of LPSs from PJ strains and S. typhimurium agreed with those of Skidmore et al (20). On the other hand, Wu and Heath (23) reported that bacterial LPS occurs in the outer cell-envelope mem-brane exclusively in the form of LPS-protein and that isolation of LPS from E. coli by the hot aqueous phenol extraction procedure results in partial degradation of this complex macromolecule. Therefore, there is a possibility that LPS extracted by Westphal's method has a low protein content, that is, lipid A-associated protein (LAP).…”

Section: Discussionsupporting

confidence: 81%

Relationship between Luminous Fish and Symbiosis

Kuwae

Andoh

Fukasawa

et al. 1983

Microbiology and Immunology

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In order to investigate the relationship between host and symbiosis in the luminous marine fish, Physiculus japonicus, the bacteriallipopolysaccharides (LPS) of symbiotic luminous bacteria were compared serologically and electrophoretically.Five symbiotic luminous bacteria (PJ strains) were separately isolated from five individuals of this fish species caught at three points, off the coasts of Chiba, Nakaminato, and Oharai, LPS preparations were made from these bacteria by Westphal's phenol-water method and highly purified by repeated ultracentrifugation. These LPSs contained little or no 2-keto-3-deoxyoctonate and had powerful mitogenic activity.In sodium dodecylsulfate polyacrylamide gel electrophoresis, these PJ-I to -5 LPSs were separated by their electrophoretic patterns into three groups; the first group included PJ-I and PJ-4, the second group PJ-2 and PJ-3, and the third group PJ-5 alone. The results agreed with those of the double immunodiffusion test; precipitin lines completely coalesced within each group but not with other groups.In immunoelectrophoresis, one precipitin line was observed between anti PJ-2 LPS serum and PJ-5 LPS but the electrophoretic mobility of PJ-5 LPS was clearly different from that of the PJ-2 LPS group. Furthermore, in a 50% inhibition test with PJ-2 LPS by the passive hemolysis system, the doses ofPJ-2 LPS, PJ-3 LPS, and PJ-5 LPS required for 50% inhibition (ID5o) in this system were 0.25, 0.25, and 21.6 pg/ml for each alkali-treated LPS, respectively, and the ID50's of both PJ-I LPS and PJ-4 LPS were above 1,000 pg/ml. These results indicate that PJ-5 LPS has an antigenic determinant partially in common with LPS from the PJ-2 group but not with LPS from the PJ-I group and that the symbiotic luminous bacterium PJ-5 is more closely related to the PJ -2 group than to the PJ -I group.These results show that the species Physiculus japonicus is symbiotically associated with at least three immunologically different strains ofluminous marine bacteria in its specialized light organ. 847

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“…While full characterization of EP is yet to be done before firm conclusions may be drawn, at the moment it would appear that EP and the protein of Wober and Alaupovi6 are probably one and the same. Other workers have also isolated proteins or lipoproteins from various gram-negative organisms (22)(23)(24), however, the activity of these materials on lymphocytes has not been tested. More recently Melchers et al (25) found that murein-associated lipoprotein isolated by Braun and Rehn (26) to be a mitogen for C3H/HeJ lymphocytes.…”

Section: Discussionmentioning

confidence: 99%