title: Purification and partial characterization of a type-specific antigen of Rickettsia tsutsugamushi.
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.
authors.affiliation: Department of Microbiology, Niigata College of Pharmacy, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Ohashi
authors.forename: A
authors.initials: A
authors.lastname: Tamura
authors.forename: M
authors.initials: M
authors.lastname: Ohta
authors.forename: K
authors.initials: K
authors.lastname: Hayashi
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000942:Antigens, Bacterial / Q000302:isolation & purification*; D000954:Antigens, Surface / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012285:Orientia tsutsugamushi / Q000032:analysis / Q000276:immunology*
chemical_list: D000596:Amino Acids; D000942:Antigens, Bacterial; D000954:Antigens, Surface