Author(s): de Wit MY, Klatser PR, de Wit MY, Klatser PR
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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.
This article was published in J Gen Microbiol
and referenced in Molecular Biology: Open Access