Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidiamalaca traust. Hemagglutinins
Identifieur interne : 001375 ( Istex/Curation ); précédent : 001374; suivant : 001376Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidiamalaca traust. Hemagglutinins
Auteurs : Nicol Parrinello ; Calogero CanicattìSource :
- Developmental and Comparative Immunology [ 0145-305X ] ; 1982.
Abstract
The carbohydrate specificities of Ascidiamalaca serum hemagglutinins were determined by hemagglutination inhibition tests. Analysis of agglutinins against rabbit and human A, B, O erythrocytes suggests that the size of the combining site corresponds to a disaccharide with a specificity for saccharides containing a D-galacto configuration (D-melibiose, D-raffinose, D-galactose, α-lactose, lactulose, L-arabinose). No anomeric specificity was observed with oligosaccharides. Hydroxyl groups probably involved in hydrogen-bond formation with agglutinin binding site, were identified as carbons C2, C4, C5 and C6 of D-galactose. Absorption experiments showed that two distinct agglutinins with similar sugar specificity ranges were responsible for rabbit and human erythrocyte agglutination. The D-galactose specificity of the agglutinins allowed the isolation, by biospecific affinity chromatography of the serum, of a protein fraction demonstrated by polyacrylamide gel electrophoresis.
Url:
DOI: 10.1016/0145-305X(82)90007-6
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Nicol Parrinello<affiliation><mods:affiliation>Institute of Zoology, University of Palermo, Via Archirafi 18, 90123 Palermo Italy</mods:affiliation>
<wicri:noCountry code="subField">90123 Palermo Italy</wicri:noCountry>
</affiliation>
<affiliation><mods:affiliation>Institute of Zoology, University of Palermo, Via Archirafi 18, 90123 Palermo Italy</mods:affiliation>
<wicri:noCountry code="subField">90123 Palermo Italy</wicri:noCountry>
</affiliation>
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<front><div type="abstract" xml:lang="en">The carbohydrate specificities of Ascidiamalaca serum hemagglutinins were determined by hemagglutination inhibition tests. Analysis of agglutinins against rabbit and human A, B, O erythrocytes suggests that the size of the combining site corresponds to a disaccharide with a specificity for saccharides containing a D-galacto configuration (D-melibiose, D-raffinose, D-galactose, α-lactose, lactulose, L-arabinose). No anomeric specificity was observed with oligosaccharides. Hydroxyl groups probably involved in hydrogen-bond formation with agglutinin binding site, were identified as carbons C2, C4, C5 and C6 of D-galactose. Absorption experiments showed that two distinct agglutinins with similar sugar specificity ranges were responsible for rabbit and human erythrocyte agglutination. The D-galactose specificity of the agglutinins allowed the isolation, by biospecific affinity chromatography of the serum, of a protein fraction demonstrated by polyacrylamide gel electrophoresis.</div>
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