Purification of the lipophosphoglycan from two Leishmania mexicana strains by lectin affinity chromatography

被引：6

作者：

Gorocica, P

Monroy, A

Rivas, B

EstradaParra, S

Leroy, Y

Chavez, R

Zenteno, E

机构：

[1] NATL AUTONOMOUS UNIV MEXICO,FAC MED,DEPT BIOQUIM,LAB INMUNOL,MEXICO CITY 04510,DF,MEXICO

[2] INST NACL ENFERMEDADES RESP,DEPT BIOQUIM,MEXICO CITY,DF,MEXICO

[3] IMSS,CTR INVEST ORIENTE,PUEBLA,MEXICO

[4] INST POLITECN NACL,DEPT INMUNOL,ESCUELA NACL CIENCIAS BIOL,MEXICO CITY,DF,MEXICO

[5] UNIV SCI & TECHNOL LILLE,UMR 111,CHIM BIOL LAB,VILLENEUVE DASCQ,FRANCE

来源：

PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY | 1997年 / 27卷 / 01期

关键词：

D O I：

10.1080/10826069708001274

中图分类号：

Q5 [生物化学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Two lipophosphoglycans (LPG) from two Leishmania mexicana (Soberano and Yucatan) strains, isolated in Mexico, were purified by affinity chromatography with the Con A lectin. The LPG from each strain, with a 10 kDa molecular weight, possesses two fractions: one with high mannose concentrations and the other with a more heterogeneous saccharidic composition; the mannose-rich fraction and the heterogeneous fraction from the Yucatan strain show a single band of identity with rabbit IgG against promastigotes from L. mexicana Yucatan. Antigen recognition was abolished by treating the high mannose LPGs with alpha-mannosidase. The presence of non reductor alpha-mannose sequences, as determinant epitopes in L. mexicana Soberano and Yucatan strains, was determined by mass spectrometry analysis and enzymatic cleavage.

引用

页码：1 / 17

页数：17

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