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. 1983 Feb 1;209(2):497–503. doi: 10.1042/bj2090497

Isolation and characterization of dermatan sulphate proteoglycan from human uterine cervix.

N Uldbjerg, A Malmström, G Ekman, J Sheehan, U Ulmsten, L Wingerup
PMCID: PMC1154117  PMID: 6847631

Abstract

Proteoglycans were extracted from human uterine cervix with 4 M-guanidinium chloride in the presence of proteinase inhibitors. They were purified by density-gradient centrifugation in 4 M-guanidinium chloride/CsCl (starting density 1.32 g/ml) followed by DEAE-cellulose and Sepharose chromatography. Only one polydisperse proteoglycan was found. s020,w was 2.1S and the weight-average molecular weight was 73 000 (sedimentation-equilibrium centrifugation) to 110 500 (light-scattering). The core protein was monodisperse, with an apparent molecular weight of 47 000. The proteoglycan contained about 30% protein and probably two or three glycosaminoglycan side chains per molecule. High contents of aspartate, glutamate and leucine were found. The glycan moiety of the proteoglycan was exclusively dermatan sulphate, with a co-polymeric structure with approximately equal quantities of iduronic acid- and glucuronic acid-containing disaccharides.

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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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