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.
Montaño
L F
LF
Depto Biología Celular, Instituto Nacional de Cardiología, Tlalpan, México.
Massó
F
F
Páez
A
A
Sandoval
S
S
Vázquez
L
L
Sánchez
L
L
Fournet
B
B
Zenteno
E
E
D000907:Antibodies, Bacterial / Q000276:immunology; D000941:Antigens / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification*; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D015151:Immunoblotting; D037102:Lectins / Q000378:metabolism; D008970:Molecular Weight; D009169:Mycobacterium tuberculosis / Q000276:immunology*
D000907:Antibodies, Bacterial; D000941:Antigens; D002241:Carbohydrates; D037102:Lectins