Abstract
An Mr = 524,000 oligomeric protein was isolated from bovine cartilage and designated COMP (Cartilage Oligomeric Matrix Protein). The protein is composed of disulfide-bonded subunits with an apparent Mr of 100,000 each. It is markedly anionic, probably due to its high contents of aspartic acid and glutamic acid, as well as to its substitution with negatively charged carbohydrates. COMP was found in all cartilages analyzed, but could not be detected in other tissues by enzyme-linked immunosorbent assay of guanidine HCl extracts. Within a given cartilage, COMP shows a preferential localization to the territorial matrix surrounding the chondrocytes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / analysis
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Animals
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Carbohydrates / analysis
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Cartilage, Articular / chemistry*
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Cartilage, Articular / cytology
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Cattle
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Centrifugation, Density Gradient
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Chromatography, DEAE-Cellulose
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Chromatography, Gel
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Electrophoresis, Polyacrylamide Gel
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Enzyme-Linked Immunosorbent Assay
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Extracellular Matrix Proteins*
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Glycoproteins / analysis
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Glycoproteins / chemistry*
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Glycoproteins / isolation & purification
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Immunoenzyme Techniques
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Macromolecular Substances
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Matrilin Proteins
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Molecular Weight
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Rats
Substances
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Amino Acids
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Carbohydrates
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Extracellular Matrix Proteins
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Glycoproteins
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Macromolecular Substances
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Matrilin Proteins