Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity.

Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity.
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从蚕豆(Vicia faba)中纯化糖蛋白凝集素,并将其特性与具有相似特异性的凝集素进行比较。

DOI:
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发表时间:
1976
影响因子:
4.1
通讯作者:
A. Neuberger
A. Neuberger
中科院分区:
生物学3区
文献类型:
--
作者:
A. K. Allen;N. N. Desai;A. Neuberger

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1.来自蚕豆(Vicia faba)的凝集素通过亲和色谱法纯化,所述亲和色谱法使用通过氨基共价连接至CH-琼脂糖(琼脂糖的ω-己酸衍生物)的3-O-甲基葡糖胺。其组成和亚基的性质进行了比较刀豆球蛋白A和豌豆和扁豆凝集素。2.与其他三种凝集素不同,蚕豆凝集素是一种糖蛋白;含有葡糖胺和甘露糖的糖肽从蛋白水解消化物中分离出来。3.分子量约为47500;糖蛋白由两个明显相同的亚基组成,通过非共价力保持在一起。片段的亚基,类似于那些发现在伴刀豆球蛋白A和大豆凝集素,被发现在活性制剂。4.将蚕豆凝集素与伴刀豆球蛋白A和豌豆、扁豆凝集素进行比较,研究单糖、单糖甲醚、二糖和糖肽对它们的抑制作用。最显著的差异涉及3-O-取代单糖,它们是蚕豆、豌豆和扁豆凝集素作用的强抑制剂,但不抑制伴刀豆球蛋白A的作用。然而,3-O-连接的二糖对这些凝集素的作用没有强烈的抑制作用。
1. The lectin from the broad bean (Vicia faba) was purified by affinity chromatography by using 3-O-methylglucosamine covalently attached through the amino group to CH-Sepharose (an omega-hexanoic acid derivative of agarose). Its composition and the nature of its subunits were compared with concanavalin A and the lectins from pea and lentil. 2. Unlike the other three lectins, broad-bean lectin is a glycoprotein; a glycopeptide containing glucosamine and mannose was isolated from a proteolytic digest. 3. The mol.wt. is about 47500; the glycoprotein consists of two apprently identical subunits, held together by non-covalent forces. Fragments of the subunits, similar to those found in concanavalin A and soya-bean agglutinin, were found in active preparations. 4. Broad-bean lectin was compared with concanavalin A and the lectins from pea and lentil in an investigation of the inhibition of their action by a number of monosaccharides, methyl ethers of monosaccharides, disaccharides and glycopeptides. The most striking differences concern 3-O-substituted monosaccharides, which are strong inhibitors of the action of broad-bean, pea and lentil lectins but not of the action of concanavalin A. There is, however, no strong inhibition of the action of these lectins by 3-Olinked disaccharides.