Erythroagglutinin from Phaseolus coccineus Var. Alubia: Chemical Characterization, Sugar Specificity, and Effect on Blood Coagulation Factors
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- 作者：Eduardo Pé ; rez-Campos ; Ricardo Lascurain ; Claudia Sierra ; Blanca Espinosa ; Henri Debray ; Stephane Bouquelet ; and Edgar Zenteno
- 刊名：Journal of Agricultural and Food Chemistry
- 出版年：1997
- 出版时间：October 1997
- 年：1997
- 卷：45
- 期：10
- 页码：3747 - 3752
- 全文大小：115K
- 年卷期：v.45,no.10(October 1997)
- ISSN：1520-5118
文摘
Purification of the erythroagglutinin from Phaseoluscoccineus var. Alubia was achieved byaffinitychromatography on human 
1-acid glycoprotein and by ionexchange chromatography. The lectinis a tetrameric glycoprotein of 31 kDa/subunit with 8% sugar byweight, which agglutinateserythrocytes without serological specificity and is devoid of mitogenicactivity toward humanperipheral lymphocytes. The specificity of the erythroagglutininis directed toward the Gal (
1-4)or (1-3) GlcNAc (1-2) Man (1-) saccharidic sequencepresent in bi- or triantennary N-acetyllactosamine-type N-glycopeptides or related glycans.Alubia erythroagglutinin inhibits thegeneration of human thrombin, very probably by protecting prothrombinfrom enzymatic cleavage.Keywords: Phaseolus coccineus lectin; glycoproteins; lectin sugarspecificity; coagulation factors
1-acid glycoprotein and by ionexchange chromatography. The lectinis a tetrameric glycoprotein of 31 kDa/subunit with 8% sugar byweight, which agglutinateserythrocytes without serological specificity and is devoid of mitogenicactivity toward humanperipheral lymphocytes. The specificity of the erythroagglutininis directed toward the Gal (1-4)or (1-3) GlcNAc (1-2) Man (1-) saccharidic sequencepresent in bi- or triantennary N-acetyllactosamine-type N-glycopeptides or related glycans.Alubia erythroagglutinin inhibits thegeneration of human thrombin, very probably by protecting prothrombinfrom enzymatic cleavage.Keywords: Phaseolus coccineus lectin; glycoproteins; lectin sugarspecificity; coagulation factors