title: Purification and characterization of a 36 kDa antigen of Mycobacterium leprae.
abstract: A 36 kDa antigen of Mycobacterium leprae was purified by phenol biphasic partition followed by preparative SDS-PAGE. The purified antigen appeared as a single band in SDS-PAGE and eluted as a single peak in ion-exchange chromatography. The antigen comprised epitopes which were cross-reactive with M. tuberculosis, as well as a species-specific epitope (recognized by MAb F47-9). Different treatments of the 36 kDa antigen suggested it to be largely protein in nature; the amino acid composition of 81% of the antigen was determined. A majority of sera from leprosy patients contained antibodies recognizing the 36 kDa antigen.
authors.affiliation: N. H. Swellengrebel Laboratory of Tropical Hygiene, Royal Tropical Institute, Amsterdam, The Netherlands.
authors.forename: M Y
authors.initials: MY
authors.lastname: de Wit
authors.forename: P R
authors.initials: PR
authors.lastname: Klatser
mesh_terms: D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial / Q000276:immunology / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006801:Humans; D007918:Leprosy / Q000276:immunology; D009166:Mycobacterium leprae / Q000276:immunology*
chemical_list: D000911:Antibodies, Monoclonal; D000942:Antigens, Bacterial