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. 1986 Mar 1;234(2):381–389. doi: 10.1042/bj2340381

Ultrastructure and composition of bovine conglutinin.

C J Strang, H S Slayter, P J Lachmann, A E Davis 3rd
PMCID: PMC1146576  PMID: 3718473

Abstract

Conglutinin binds in a Ca2+-dependent manner to the carbohydrate portion of zymosan and cell-bound iC3b (complement subcomponent C3b cleaved by Factor I in the presence of factor H) similarly to lectin-like proteins that participate in the clearance of plasma glycoproteins. This carbohydrate-binding protein has been found to include both collagenous and non-collagenous domains. Electron micrographs of bovine conglutinin are presented in which conglutinin appears as a tetramer of four 'lollipop' structures emanating from a central hub. The stem region, linking each head to the central hub, is quite stiff, whereas the hub-stem junction is a flexible hinge. From electron micrographs of a pepsin digest of conglutinin, the linkage region is identified as the collagenous portion of the macromolecule. Conglutinin is a multimer of a single polypeptide chain. From sedimentation equilibria of unreduced as compared with reduced and alkylated conglutinin, there are determined to be three disulphide-linked chains. These data, combined with information on the subunit polypeptide of conglutinin, suggest a model for conglutinin in which four disulphide-linked trimers are associated via the N-termini to form the intact macromolecule as viewed in the electron microscope. The ultrastructure of conglutinin appears ideally suited to its lectin-like function.

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