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Carbohydrate binding specificity and purification by biospecific affinity chromatography of Ascidia malaca Traust. hemagglutinins.

Abstract：

: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.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Parrinello N,Canicattì C

doi

10.1016/0145-305x(82)90007-6

subject

Has Abstract

pub_date

1982-01-01 00:00:00

pages

53-64

issue

1

eissn

0145-305X

issn

1879-0089

pii

0145-305X(82)90007-6

journal_volume

6

pub_type

杂志文章

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