BINDING OF THE GALACTOSE-SPECIFIC PSEUDOMONAS-AERUGINOSA LECTIN, PA-I, TO GLYCOSPHINGOLIPIDS AND OTHER GLYCOCONJUGATES

被引：38

作者：

LANNE, B ^{[1
]}

CIOPRAGA, J ^{[1
]}

BERGSTROM, J ^{[1
]}

MOTAS, C ^{[1
]}

KARLSSON, KA ^{[1
]}

机构：

[1] ACAD ROMANA, INST BIOCHEM, BUCHAREST, ROMANIA

来源：

GLYCOCONJUGATE JOURNAL | 1994年 / 11卷 / 04期

关键词：

GLYCOCONJUGATE BINDING; NEO-GLYCOPROTEIN; SACCHARIDE INHIBITION;

D O I：

10.1007/BF00731201

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：

The carbohydrate-binding specificity of Pseudomonas aeruginosa lectin I (PA-I) in iodinated or biotinylated form was studied. A large number of glycosphingolipids, as well as some glycoproteins and neoglycoproteins were used as ligands. Also, inhibition by free saccharides of PA-I binding to glycosphingolipids was tested. It was found that the lectin binds most strongly to terminal and nonsubstituted Gal alpha 3Gal- or Gal alpha 4Gal-structures.

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页码：292 / 298

页数：7

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