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.
BT - Journal of general microbiology C1 - http://www.ncbi.nlm.nih.gov/pubmed/3065448?dopt=Abstract DA - 1988 Jun DO - 10.1099/00221287-134-6-1541 IS - 6 J2 - J. Gen. Microbiol. LA - eng N2 -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.
PY - 1988 SP - 1541 EP - 8 T2 - Journal of general microbiology TI - Purification and characterization of a 36 kDa antigen of Mycobacterium leprae. VL - 134 SN - 0022-1287 ER -