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. 1988 Nov 15;256(1):61–68. doi: 10.1042/bj2560061

Purification and characterization of the core-specific lectin from human serum and liver.

K J Colley 1, M C Beranek 1, J U Baenziger 1
PMCID: PMC1135368  PMID: 3223912

Abstract

A lectin that displays specificity for the core region of asparagine-linked oligosaccharides (Man3GlcNAc2-Asn) was isolated from human serum and liver by affinity chromatography on mannan-Sepharose. The designation 'core-specific lectin' (CSL) is used to indicate its specificity. Selective elution of human CSL from mannan-Sepharose was accomplished with 50 mM-mannose. Two additional proteins that displayed Ca2+-dependent binding to mannan-Sepharose were eluted by mannose 6-phosphate or beta-glycerophosphate but not by mannose. The latter proteins were identified as C-reactive protein and serum amyloid protein. Human CSL isolated from liver was indistinguishable from serum CSL in its physicochemical properties, immunological properties and specificity. The N-terminal sequence of human CSL is homologous to that reported for 'mannan-binding protein C' (MBP-C) [Drickamer, Dordal & Reynolds (1986) J. Biol. Chem. 261, 6878-6887]. The amino acid composition of human CSL is similar to that of rat MBP-C, including the presence of hydroxyproline and hydroxylysine residues. Collagen-like sequences with hydroxylated proline and lysine residues appear to be present in human CSL as well as in rat CSL. The collagen-like regions of human and rat CSL may play a role in assembly of CSL subunits into complexes consisting of nine subunits that display Ca2+-dependent carbohydrate-binding activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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