Literature DB >> 6787136

An improved method for the isolation of the major protein of the gonococcal outer membrane in an antigenically reactive form.

L T James, J E Heckels.   

Abstract

The major outer membrane protein (protein I) has been isolated from Neisseria gonorrhoeae strain P9 in an immunologically reactive form. Membranes were sequentially extracted with the detergents sodium cholate and Empigen BB. Protein I was enriched in the Empigen-soluble fraction and was separated from other proteins and lipopolysaccharide by gel filtration chromatography on Sephadex G-200. The purified protein retained its antigenic activity with antiserum raised against the unfractionated outer membrane complex.

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Year:  1981        PMID: 6787136     DOI: 10.1016/0022-1759(81)90152-6

Source DB:  PubMed          Journal:  J Immunol Methods        ISSN: 0022-1759            Impact factor:   2.303


  2 in total

1.  Sequence polymorphism, predicted secondary structures, and surface-exposed conformational epitopes of Campylobacter major outer membrane protein.

Authors:  Q Zhang; J C Meitzler; S Huang; T Morishita
Journal:  Infect Immun       Date:  2000-10       Impact factor: 3.441

2.  Expression of large amounts of neisserial porin proteins in Escherichia coli and refolding of the proteins into native trimers.

Authors:  H L Qi; J Y Tai; M S Blake
Journal:  Infect Immun       Date:  1994-06       Impact factor: 3.441

  2 in total

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