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J Gen Microbiol. 1988 Jun;134(6):1541-8.

Purification and characterization of a 36 kDa antigen of Mycobacterium leprae.

Author information

1
N. H. Swellengrebel Laboratory of Tropical Hygiene, Royal Tropical Institute, Amsterdam, The Netherlands.

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.

PMID:
3065448
DOI:
10.1099/00221287-134-6-1541
[Indexed for MEDLINE]

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