An antigenic complex has been isolated in a highly purified from from the Melvin strain of Neisseria gonorrhoeae. The complex has a molecular weight of 9.3 × 10 6 and on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was found to consist of several subunits; the most predominant had the following molecular weights: 110,000, 94,000, 68,000, a smear containing (52,000, 48,000, and 44,000), 42,000, 36,000, 29,000, 28,000, 26,000, and 12,000 comprising 89% of the total protein. With the exception of the subunit of molecular weight 110,000, no change in the content or the mobility of other subunits was observed when β-mercaptoethanol was omitted from the denaturation solution of sodium dodecyl sulfate electrophoresis. Amino acid analysis of the complex showed a predominance of hydrophobic amino acids. These data implicated noncovalent interactions between the subunits. When the cells were labeled with fluorescamine it was possible to obtain a fluorescent complex with identical properties. Among several buffers used for the isolation of the complex, 0.2 M tris(hydroxymethyl)aminomethane buffer (pH 7.5) gave maximum yield with low amounts of lipopolysaccharide and phospholipid; the choice of the buffer for column chromatography did not seem to make any difference. The high protein content and low amounts of lipopolysaccharide and phospholipid are characteristic properties of the complex.

An antigenic subunit of molecular weight 66,000 daltons has been isolated from the antigenic complex of the Melvin strain of Neisseria gonorrhoeae. Incubation of the complex in 8M urea at room temperature for four hours resulted in the dissociation of the subunit from the complex. It was separated from the complex by chromatography of the incubation mixture on a Sepharose 6B column in 50 mM ammonium bicarbonate pH 8.5 without 8M urea and further purified by affinity chromatography. This communication reports on a newly isolated antigenic protein devoid of LPS present in the bacteria.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTAllergic encephalomyelitis: evidence for lack of significant encephalitogenic activity of purified peptide L in the monkeyYashwant D. Karkhanis, Johanna Y. Zeltner, Richard L. Anderson, and Dennis J. CarloCite this: Biochemistry 1978, 17, 21, 4571–4577Publication Date (Print):October 17, 1978Publication History Published online1 May 2002Published inissue 17 October 1978https://pubs.acs.org/doi/10.1021/bi00614a032https://doi.org/10.1021/bi00614a032research-articleACS PublicationsRequest reuse permissionsArticle Views22Altmetric-Citations2LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts