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. 1989 May;57(5):1427–1431. doi: 10.1128/iai.57.5.1427-1431.1989

Purification and partial characterization of a type-specific antigen of Rickettsia tsutsugamushi.

N Ohashi 1, A Tamura 1, M Ohta 1, K Hayashi 1
PMCID: PMC313294  PMID: 2496028

Abstract

A type-specific antigen (54- to 56-kilodalton polypeptide) in the envelope of Rickettsia tsutsugamushi was purified from each of three prototype strains (Gilliam, Karp, and Kato) by a combination of mild anionic detergent treatment, gel filtration, and reverse-phase high-performance liquid chromatography. The purified antigens from the three strains were shown to have similar amino acid compositions: primarily aspartic acid, glutamic acid, and glycine, with lesser amounts of cysteine, methionine, and tyrosine. The N-terminal amino acid sequences of the antigens were 74.3% homologous among the three strains.

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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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