Lectin-binding properties of different Leishmania species
Lectin-binding properties of different Leishmania species
复制标题
DOI：
10.1007/s004360050597
复制
发表时间：
1999-07-01
影响因子：
2
通讯作者：
Saraiva, FMB
中科院分区：
文献类型：
--
作者：
Andrade, AFB;Saraiva, FMB
Carbohydrate cell-surface residues on stationary promastigotes of 19 isolates of Leishmania were studied with a panel of 27 highly purified lectins, which were specific for N-aceryl-D-glucosamine, D-mannose, L-fucose, D-galactose, N-acetyl-D-galactosamine, and sialic acid. The specificity of the cell-surface carbohydrates was analyzed by agglutination and radioiodinated lectin-binding assays. L. (L.) amazonensis and L. (L.) donovani were agglutinated by 12 and 10 of the 27 lectins used, respectively. Artocarpus integrifolia lectin (Jacalin) was incapable of agglutinating the tested species of the donovani complex, and this result was confirmed by radioiodinated Jacalin-binding assays. Jacalin had an average of 3.8 x 10(6) receptors/L. (L) amazonensis promastigote and bound with an association constant of 5 x 10(6) M-1.
