Journal of Biological Chemistry · 1992 · 527 citations · 21 references
Life SciencesBiochemistryMolecular BiologyGlycobiologyProteomicsStructural BiologyArticular Cartilage StructureCartilage BiologyExtracellular MatrixExtracellular Matrix GlycansGlobular ProteinsAggrecan BiologyArticular Cartilage ProteoglycansCartilage Extracellular MatrixDisulfide-bonded Protein ComplexesExtracellular Matrix ProteinsGlycoproteins Of The Extracellular MatrixProteoglycan DistributionProteoglycans
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.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations