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. 1989 Jun;57(6):1849–1853. doi: 10.1128/iai.57.6.1849-1853.1989

Relatedness of structures of a major immunogen in Trichomonas vaginalis isolates.

J F Alderete 1, K A Neale 1
PMCID: PMC313366  PMID: 2785964

Abstract

Solubilization of live Trichomonas vaginalis organisms with detergent caused the release of cysteine proteinases in the detergent extract which were inhibitable with N-alpha-p-tosyl-L-lysine chloromethyl ketone. The detergent extracts of all isolates tested possessed similar cysteine proteinase activities. These parasite proteinases rapidly degraded a prominent immunogen whose surface disposition undergoes phenotypic variation in some isolates. The relatedness of the forms of this immunogen among all isolates tested was confirmed by identical immunoblot patterns of autolysed immunogen, and data suggest the presence of repeating units or at least equidistant sites for proteinase cleavage within the immunogen molecule.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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