Extractable proteoglycan from human femoral-head articular cartilage
| Autor: | C F Phelps, M I V Jayson, D W Bullimore |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1981 |
| Předmět: |
Cartilage
Articular Male Adolescent Hydrochloride Macromolecular Substances Magnesium Chloride Cleavage (embryo) Biochemistry Guanidines chemistry.chemical_compound Column chromatography Centrifugation Density Gradient Humans Centrifugation Magnesium Hyaluronic Acid Molecular Biology Guanidine Chromatography biology Chemistry Temperature Infant Femur Head Cell Biology Middle Aged Monomer Proteoglycan Models Chemical biology.protein Radius of gyration Chromatography Gel Female Proteoglycans Particle size Research Article |
| Popis: | Proteoglycans were prepared from human femoral-head articular cartilage by using either guanidinium hydrochloride or MgCl2 as extractant, followed by density-gradient centrifugation. The proteoglycan subunit had a particle weight of 2.6 x 10(6), with a radius of gyration, RG, of 68.5 nm in 150 mM-NaCl/20 mM-sodium phosphate buffer, pH 7.0. The proteoglycan aggregate had a particle weight of 3.7 x 10(6) (RG 84 nm) for guanidinium hydrochloride extracts and 8.7 x 10(6) (RG 118 nm) for MgCl2 extracts in the same buffer. The addition of excess of high-molecular-weight hyaluronate did not significantly alter the particle size of the aggregate. The small increase in size probably reflects a rapid equilibrium between hyaluronate and proteoglycan monomers, and is not due to proteolytic cleavage producing non-aggregating units. Experiments that support the rapid-interaction hypothesis include analytical ultracentrifugation and column chromatography. This interaction does not appear to be pressure-sensitive at 20 degrees C, but is sensitive to temperature variation near the physiological range. |
| Databáze: | OpenAIRE |
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