Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin

被引：54

作者：

Yagi, F ^{[1
]}

Miyamoto, M ^{[1
]}

Abe, T ^{[1
]}

Minami, Y ^{[1
]}

Tadera, K ^{[1
]}

Goldstein, IJ ^{[1
]}

机构：

[1] UNIV MICHIGAN,DEPT BIOL CHEM,ANN ARBOR,MI 48109

来源：

GLYCOCONJUGATE JOURNAL | 1997年 / 14卷 / 02期

关键词：

Agrocybe cylindracea; fungal lectin; carbohydrate-binding specificity; sialic acid-containing carbohydrate chain;

D O I：

10.1023/A:1018558225454

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A lectin was isolated from fruiting bodies of Agrocybe cylindracea by two ion-exchange chromatographies and gel filtration on Toyopearl HW55F. The lectin was homogeneous on polyacrylamide gel electrophoresis and its molecular mass was determined to be 30 000 by gel filtration, and 15 000 by sodium dodecylsulfate polyacrylamide gel electrophoresis, signifying a dimeric protein. Its carbohydrate-binding specificity was investigated both by sugar-hapten inhibition of hemagglutination and by enzyme-linked immunosorbent assay. The inhibition tests showed the affinity of the lectin to be weakly directed toward sialic acid and lactose, and the enhanced affinity toward trisaccharides containing the NeuAc alpha 2,3Gal beta-structure. Importantly, the lectin strongly interacted with glycoconjugates containing NeuAc alpha 2,3Gal beta 1,3GlcNAc-/GalNAc sequences.

引用

页码：281 / 288

页数：8

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