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Literature DB >> 623781

Isolation and chemical characterization of two distinct "link proteins" from bovine nasal cartilage proteoglycan complex.

Abstract

Bovine nasal cartilage proteoglycan aggregates have been dissociated and separated by dissociative density gradient centrifugation into proteoglycan sub-units and "link fraction". The latter contained mainly the two "link proteins" as shown by analytical sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The two "link proteins" were then separated by preparative gel electrophoresis under dissociative conditions. Molecular weight and amino acid composition of both proteins are presented.

Entities: Chemical Disease Species

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Year: 1978 PMID： 623781 DOI： 10.1016/0005-2795(78)90578-0

Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002

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Cited

13 in total

1. A study of equilibrium binding of link protein to hyaluronate.

Authors: M Lyon; I A Nieduszynski
Journal: Biochem J Date: 1983-08-01 Impact factor: 3.857

2. Isolation and biochemical characterization of the tryptic fragments of bovine nasal-cartilage proteoglycan monomer of high buoyant density.

Authors: H D Keiser; J B Adlersberg; H M Steinman
Journal: Biochem J Date: 1982-06-01 Impact factor: 3.857

9. Expression of reduced amounts of structurally altered aggrecan in articular cartilage chondrocytes exposed to high hydrostatic pressure.

Authors: M J Lammi; R Inkinen; J J Parkkinen; T Häkkinen; M Jortikka; L O Nelimarkka; H T Järveläinen; M I Tammi
Journal: Biochem J Date: 1994-12-15 Impact factor: 3.857

10. A comparative study of the binding of cartilage link protein and the hyaluronate-binding region of the cartilage proteoglycan to hyaluronate-substituted Sepharose gel.

Authors: A Tengblad
Journal: Biochem J Date: 1981-11-01 Impact factor: 3.857

Isolation and chemical characterization of two distinct "link proteins" from bovine nasal cartilage proteoglycan complex.

1. A study of equilibrium binding of link protein to hyaluronate.

2. Isolation and biochemical characterization of the tryptic fragments of bovine nasal-cartilage proteoglycan monomer of high buoyant density.

3. The role of link-protein in the structure of cartilage proteoglycan aggregates.

4. The origin of human cartilage proteoglycan link-protein heterogeneity and fragmentation during aging.

5. Link-proteins and non-collagenous proteins from normal and chondrodysplastic cartilages.

6. Comparative studies on human and bovine nasal cartilage proteoglycan complex components.

7. Age-related changes in the structure of proteoglycan link proteins present in normal human articular cartilage.

8. Structure and interactions of cartilage proteoglycan binding region and link protein.

9. Expression of reduced amounts of structurally altered aggrecan in articular cartilage chondrocytes exposed to high hydrostatic pressure.

10. A comparative study of the binding of cartilage link protein and the hyaluronate-binding region of the cartilage proteoglycan to hyaluronate-substituted Sepharose gel.