Trowbridge I S
Proc Natl Acad Sci U S A. 1973 Dec;70(12):3650-4. doi: 10.1073/pnas.70.12.3650.
A mitogenic lectin that has a carbohydrate-binding specificity similar to that of concanavalin A (Con A) can be isolated from pea seeds. Chemical modification (succinylation, acetylation, or treatment with the diazonium salt of sulfanilic acid), changes its biological properties. In mitogenic stimulation of mouse spleen cells and in hemagglutination, the differences between the chemically modified pea lectin and the native molecule are similar to those observed between succinyl-Con A and native Con A. However, whereas chemical modification converts tetrameric Con A to a dimeric molecule, similar treatments of the pea lectin do not change its quaternary structure. The results of binding studies of the pea lectin and its derivatives to mouse spleen cells suggest that the differences in biological activities may be explained by a reduction in binding affinity of the pea lectin for glycoproteins on the spleen cell surface after chemical modification.
一种具有与伴刀豆球蛋白A(Con A)相似的碳水化合物结合特异性的促有丝分裂凝集素可从豌豆种子中分离出来。化学修饰(琥珀酰化、乙酰化或用对氨基苯磺酸重氮盐处理)会改变其生物学特性。在对小鼠脾细胞的促有丝分裂刺激和血细胞凝集过程中,化学修饰后的豌豆凝集素与天然分子之间的差异类似于琥珀酰-Con A与天然Con A之间观察到的差异。然而,化学修饰可将四聚体Con A转化为二聚体分子,而对豌豆凝集素进行类似处理并不会改变其四级结构。豌豆凝集素及其衍生物与小鼠脾细胞结合研究的结果表明,生物学活性的差异可能是由于化学修饰后豌豆凝集素对脾细胞表面糖蛋白的结合亲和力降低所致。