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Immunorecognition in the freshwater bivalve, Corbicula fluminea. II. Isolation and characterization of a plasma opsonin with hemagglutinating activity.

Abstract：

:Opsonizing and agglutinating activities of plasma from the freshwater clam, Corbicula fluminea, were found to be inhibited by the sugars, 2-deoxy-D-glucose (deoxy-Glu) and N-acetyl-D-galactosamine (GalNAc). The plasma opsonin/agglutinin was subsequently isolated by a two-step separation procedure. Aldehyde-fixed rabbit erythrocytes (RRBC) were used as a solid-phase plasma opsonin affinity absorbant, and deoxyGlu and GalNAc were used in the eluting buffer to desorb several RRBC-binding plasma proteins. The second step involved the further separation of sugar-eluted proteins by Sephacryl S-200 gel filtration. A plasma protein with an apparent molecular weight of 40 kd on SDS-PAGE under nonreducing conditions was found to possess both agglutinating and opsonizing activities. It was further shown to be composed of two identical 20 kd subunits associated through disulfide linkage(s). Although this protein shares some structural similarity with other bivalve opsonins, differences in native molecular size or subunit structure, agglutinating properties and/or sugar binding specificity support the current hypothesis that naturally occurring plasma opsonins of molluscs represent a heterogeneous group of proteins unified primarily through their lectin-like characteristic of binding specific carbohydrate determinants.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Yang R,Yoshino TP

doi

10.1016/0145-305x(90)90032-a

subject

Has Abstract

pub_date

1990-10-01 00:00:00

pages

397-404

issue

4

eissn

0145-305X

issn

1879-0089

pii

0145-305X(90)90032-A

journal_volume

14

pub_type

杂志文章

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