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

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.