6533b85bfe1ef96bd12bb559
RESEARCH PRODUCT
Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidiamalaca traust. Hemagglutinins
Calogero CanicattìNicolò Parrinellosubject
Hemagglutination Inhibition TestsErythrocytesImmunologyDisaccharideBiologyChromatography Affinitychemistry.chemical_compoundRaffinoseAgglutininSpecies SpecificityAffinity chromatographyAnimalsHumansUrochordataBinding sitePolyacrylamide gel electrophoresisBinding selectivityMelibioseBinding SitesGalactoseHemagglutination TestsHemagglutination Inhibition TestsAgglutination (biology)HemagglutininschemistryBiochemistryAntibody FormationCarbohydrate MetabolismRabbitsDevelopmental Biologydescription
The carbohydrate specificities of Ascidia malaca 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, alpha-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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1982-12-01 | Developmental & Comparative Immunology |