ISOLATION OF A 32 KDA MYCOBACTERIUM-TUBERCULOSIS PROTEIN BY LECTIN AFFINITY-CHROMATOGRAPHY

Authors
MONTANO LF MASSO F PAEZ A SANDOVAL S VAZQUEZ L SANCHEZ L FOURNET B ZENTENO E
Citation
Lf. Montano et al., ISOLATION OF A 32 KDA MYCOBACTERIUM-TUBERCULOSIS PROTEIN BY LECTIN AFFINITY-CHROMATOGRAPHY, Comparative biochemistry and physiology. B. Comparative biochemistry, 108(2), 1994, pp. 265-272
Citations number
42
Categorie Soggetti
Biology
Journal title
Comparative biochemistry and physiology. B. Comparative biochemistry → ACNP
ISSN journal
03050491
Volume
108
Issue
2
Year of publication
1994
Pages
265 - 272
Database
ISI
SICI code
0305-0491(1994)108:2<265:IOA3KM>2.0.ZU;2-K
Abstract
A 32 kDa antigen from delipidated M. tuberculosis H37Rv culture filtra te protein extract (CFPE) was purified by affinity chromatography on i mmobilized Lens culinaris lectin and electroelution. This antigen repr esents 0.4% of the total CFPE carbohydrate content and possesses galac tose, xylose, mannose and GlcNAc (5:2:3:1 mol. ratio). A monoclonal an tibody against the purified antigen reacted with the 32 kDa as well as a 30 kDa antigen in H37Rv CFPE, thus suggesting that both antigens re present closely related allelomorphic forms of the same antigen.