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Literature DB >> 6772627

Cross-linking analysis of Neisseria gonorrhoeae outer membrane proteins.

Abstract

The arrangement of proteins in the outer membrane of Neisseria gonorrhoeae was investigated through the use of cleavable chemical cross-linking reagents and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Cross-linking of isolated outer membranes yielded dimers and trimers of the major outer membrane protein. In addition, data were obtained suggesting that a stable interaction exists between the major protein I and protein II, the second most prevalent protein in the gonococcal outer membrane.

Entities: Chemical Species

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Year: 1980 PMID： 6772627 PMCID： PMC294206 DOI： 10.1128/jb.143.1.182-187.1980

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

25 in total

1. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding.

Authors: J P Rosenbusch
Journal: J Biol Chem Date: 1974-12-25 Impact factor: 5.157

2. An approach to nearest neighbor analysis of membrane proteins. Application to the human erythrocyte membrane of a method employing cleavable cross-linkages.

Authors: K Wang; F M Richards
Journal: J Biol Chem Date: 1974-12-25 Impact factor: 5.157

3. Cross-linking the major proteins of the isolated erythrocyte membrane.

Authors: T L Steck
Journal: J Mol Biol Date: 1972-05-14 Impact factor: 5.469

4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors: U K Laemmli
Journal: Nature Date: 1970-08-15 Impact factor: 49.962

5. Gel chromatography of proteins in denaturing solvents. Comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants.

Authors: W W Fish; J A Reynolds; C Tanford
Journal: J Biol Chem Date: 1970-10-10 Impact factor: 5.157

6. Cell envelope of Neisseria gonorrhoeae: outer membrane and peptidoglycan composition of penicillin-sensitive and-resistant strains.

Authors: H Wolf-Watz; T Elmros; S Normark; G D Bloom
Journal: Infect Immun Date: 1975-06 Impact factor: 3.441

5. Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers.

Authors: B L Angus; R E Hancock
Journal: J Bacteriol Date: 1983-09 Impact factor: 3.490

5 in total

Cross-linking analysis of Neisseria gonorrhoeae outer membrane proteins.

1. Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding.

2. An approach to nearest neighbor analysis of membrane proteins. Application to the human erythrocyte membrane of a method employing cleavable cross-linkages.

3. Cross-linking the major proteins of the isolated erythrocyte membrane.

4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

5. Gel chromatography of proteins in denaturing solvents. Comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants.

6. Cell envelope of Neisseria gonorrhoeae: outer membrane and peptidoglycan composition of penicillin-sensitive and-resistant strains.

7. Isolation and characterization of the outer membrane of Neisseria gonorrhoeae.

8. Studies on gonococcus infection. II. Freeze-fracture, freeze-etch studies on gonocci.

9. Studies on gonococcus infection. I. Pili and zones of adhesion: their relation to gonococcal growth patterns.

10. An outer membrane protein of Neisseria meningitidis group B responsible for serotype specificity.

1. Antigens that are similar in apparent molecular weight to gonococcal outer membrane protein III.

2. Mechanism of action of blocking immunoglobulin G for Neisseria gonorrhoeae.

3. Identification of an iron-regulated 37,000-dalton protein in the cell envelope of Neisseria gonorrhoeae.

4. Gonococcal sensitivity to fecal lipids can be mediated by an Mtr-independent mechanism.

5. Outer membrane porin proteins F, P, and D1 of Pseudomonas aeruginosa and PhoE of Escherichia coli: chemical cross-linking to reveal native oligomers.