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.
| Original language | English |
|---|---|
| Pages (from-to) | 1541-1548 |
| Journal | Journal of general microbiology |
| Volume | 134 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 1988 |
| Externally published | Yes |
UN SDGs
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SDG 3 Good Health and Well-being
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