Purification and characterization of a 36 kDa antigen of Mycobacterium leprae

J Gen Microbiol. 1988 Jun;134(6):1541-8. doi: 10.1099/00221287-134-6-1541.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal
  • Antigens, Bacterial / immunology
  • Antigens, Bacterial / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Leprosy / immunology
  • Mycobacterium leprae / immunology*

Substances

  • Antibodies, Monoclonal
  • Antigens, Bacterial