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. 1994 Jun;108(2):265-72.
doi: 10.1016/0305-0491(94)90074-4.

Isolation of a 32 kDa Mycobacterium tuberculosis protein by lectin affinity chromatography

L F Montaño  1 , F Massó, A Páez, S Sandoval, L Vázquez, L Sánchez, B Fournet, E Zenteno
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Isolation of a 32 kDa Mycobacterium tuberculosis protein by lectin affinity chromatography

L F Montaño et al. Comp Biochem Physiol Biochem Mol Biol. 1994 Jun.

Abstract

A 32 kDa antigen from delipidated M. tuberculosis H37Rv culture filtrate protein extract (CFPE) was purified by affinity chromatography on immobilized Lens culinaris lectin and electroelution. This antigen represents 0.4% of the total CFPE carbohydrate content and possesses galactose, xylose, mannose and GlcNAc (5:2:3:1 mol. ratio). A monoclonal antibody against the purified antigen reacted with the 32 kDa as well as a 30 kDa antigen in H37Rv CFPE, thus suggesting that both antigens represent closely related allelomorphic forms of the same antigen.

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