Studies on the N-terminal sequences of lectins isolated from the seeds of Butea frondosa.

Biomedical science Pub Date : 1991-01-01
S Padmanabhan, V V Demin, I N Telezhinskaya, E V Zaitseva, T B Golubeva, Chertov OYu
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Abstract

Two lectin fractions (FI and FII) were obtained from seeds of Butea frondosa by affinity chromatography on a sorbent of macroporous glass coupled to the disaccharide alpha-D-GalNAc-(1----3)-beta-D-Gal. Both of these fractions, although different in their sugar specificity, were found on SDS-PAGE to consist of two polypeptide chains of 33 kDa and 35 kDa. In the native state the subunits associated to form a 250 kDa complex, possibly comprising four molecules of the 33 kDa polypeptide and four molecules of the 35 kDa polypeptide. The presence of a faint 70 kDa band when the 250 kDa complex was subjected to SDS-PAGE may indicate the existence of a sequential mechanism of aggregation. N-terminal amino acid sequence analysis revealed extensive homology between these lectins and those of other Leguminosae.

山茶种子凝集素n端序列的研究。
采用大孔玻璃吸附双糖α - d - galnac -(1----3)- β - d - gal,用亲和层析法从Butea frondosa种子中分离得到两个凝集素组分(FI和FII)。这两个部分虽然糖特异性不同,但在SDS-PAGE上发现它们由两条33 kDa和35 kDa的多肽链组成。在天然状态下,亚基结合形成250 kDa的复合物,可能包括4个33 kDa的多肽分子和4个35 kDa的多肽分子。当250 kDa复合物进行SDS-PAGE检测时,发现70 kDa的微弱条带,这可能表明存在顺序聚集机制。n端氨基酸序列分析表明,这些凝集素与其他豆科植物的凝集素具有广泛的同源性。
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