@article{10388,
  keywords = {Antibodies, Monoclonal, Antigens, Bacterial, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Humans, leprosy, Mycobacterium leprae},
  author = {Wit M Y and Klatser P R},
  title = {Purification and characterization of a 36 kDa antigen of Mycobacterium leprae.},
  abstract = {<p>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.</p>},
  year = {1988},
  journal = {Journal of general microbiology},
  volume = {134},
  pages = {1541-8},
  month = {1988 Jun},
  issn = {0022-1287},
  doi = {10.1099/00221287-134-6-1541},
  language = {eng},
}