GALACTOSE-OXIDASE - ENZYME WITH LECTIN PROPERTIES

被引：15

作者：

HOREJSI, V

机构：

[1] Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Praha 4

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 577卷 / 02期

关键词：

Galactose oxidase; Lectin activity; Sugar binding;

D O I：

10.1016/0005-2795(79)90041-2

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：

Galactose oxidase interacts with immobilized D-galactosyl residues and related immobilized and free sugars under the conditions of affinity electrophoresis in polyacrylamide gel and agglutinates sialidase-treated human erythrocytes. The agglutination is also inhibited by D-galactose and its derivatives and is temperature dependent. The sugar binding and hemagglutinating activity are preserved after removal of Cu2+ essential for enzymic activity. These properties are very similar to those of some typical lectins; however, a number of D-galactose specific lectins do not possess any detectable galactose oxidase activity. © 1979.

引用

页码：383 / 388

页数：6

共 20 条

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