PMID: 708382Sep 1, 1978Paper

Interactions between different corneal proteoglycans

The Biochemical Journal
P SpezialeC Balduini

Abstract

Proteoglycans were extracted from bovine cornea with 4M-guanidinium chloride and purified by CsCl-density-gradient centrifugation. Under associative conditions two fractions were found: one capable of forming assemblies of high molecular weight and another lacking this property. The heavier fraction (density 1.59 g/ml) was eluted as a single retarded peak from Sepharose 2B, but on DEAE-Sephadex chromatography, gave two peaks: the first (eluted with 0.75 M-NaCl) contained mainly proteochondroitin sulphate and the second (eluted with 1.25 M-NaCl) mainly proteokeratan sulphate. Each of these proteoglycans was more retarded on Sepharose 2B than was the original sample from density-gradient centrifugation. Re-aggregation was obtained by recombination of the two fractions. The lighter fraction (density 1.44 g/ml), containing predominantly keratan sulphate chains, was eluted from DEAE-Sephadex as a single peak with 1.25 M-NaCl and was retarded on Sepharose 2B: this fraction was not able to form aggregates with proteochondroitin sulphate. Chemical analyses of the carbohydrate and protein moieties of the proteoglycans from DEAE-Sephadex confirmed that, in the cornea, different subunits are present with characteristic aggregation propert...Continue Reading

Citations

Apr 1, 1983·Experimental Eye Research·L CösterJ D Gregory
Jan 1, 1988·Tissue & Cell·A Velasco, J Hidalgo
Jun 1, 1990·Journal of Biomedical Materials Research·A LamureC Lacabanne

Related Concepts

Bos indicus
Centrifugation, Isopycnic
Chromatography, Agarose
Ion-Exchange Chromatography Procedure
Cornea
Proteoglycan Type H

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