Structural comparison of the lectin from sainfoin (Onobrychis viciifolia) with concanavalin A and other D-mannose specific lectins.

Structural comparison of the lectin from sainfoin (Onobrychis viciifolia) with concanavalin A and other D-mannose specific lectins.
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红豆甙 (Onobrychis viciifolia) 凝集素与刀豆球蛋白 A 和其他 D-甘露糖特异性凝集素的结构比较。

DOI:
10.1139/o82-120
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发表时间:
1982
期刊:
Canadian journal of biochemistry
影响因子:
--
通讯作者:
M. Yaguchi
M. Yaguchi
中科院分区:
--
文献类型:
--
作者:
N. Young;R. Williams;C. Roy;M. Yaguchi

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用Sephadex G-75亲和层析法从红豆草中制备了D-甘露糖特异性凝集素,并对其圆二色谱(CD)、金属含量、抗原性和N-末端氨基酸序列与4种豆科植物凝集素和刀豆球蛋白A进行了比较。红豆草凝集素与其他D-甘露糖特异性凝集素的亲缘关系仅略高于豆科植物凝集素。CD实验和抗原性实验也证实了这四种蚕豆凝集素的亲缘关系。N-端序列显示红豆草有两个异凝集素,在残基四处的序列不同。该序列与其他几种凝集素的N-端序列同源;因此,尽管红豆草凝集素在结构和特异性上有一些相似之处,但它不显示刀豆蛋白A特有的序列的环状排列。该区域还包含第33位的唯一半胱氨酸残基。用梯度亲和层析法研究了红豆草凝集素的碳水化合物结合特性。其对甲基α-D-葡萄糖苷的表观Ka约为10(3)M-1,接近豌豆凝集素的Ka。然而,在甲基α-D-甘露糖苷、麦芽糖和甲基α-D-葡萄糖苷的相对结合行为上,它更像刀豆蛋白A而不是豌豆凝集素。
The D-mannose specific lectin from sainfoin was prepared by affinity chromatography on Sephadex G-75, and its circular dichroism (CD), metal content, antigenic character, and N-terminal amino acid sequence were compared with those of four lectins from Vicieae plants and concanavalin A. The sainfoin lectin was only slightly more closely related to these other D-mannose specific lectins, than to lectins of leguminous plants in general. The CD and antigenic experiments also confirmed the close relationship of the four Vicieae lectins. The N-terminal sequence showed sainfoin has two isolectins, differing in sequence at residue four. The sequence was homologous to N-terminal sequences of several other lectins; hence, despite some structural and specificity similarities, the sainfoin lectin does not show the circular permutation of sequence unique to concanavalin A. This region also contained the sole cysteine residue, at position 33. The carbohydrate-binding properties of the sainfoin lectin were studied by gradient affinity chromatography. Its apparent Ka for methyl alpha-D-glucoside was approximately 10(3) M-1, close to the Ka of the pea lectin. However, in the relative binding behaviour of methyl alpha-D-mannoside, maltose, and methyl alpha-D-glucoside, it resembled concanavalin A more than the pea lectin.