Native cartilage matrix protein (CMP). A compact trimer of subunits assembled via a coiled-coil alpha-helix.
作者： N Hauser , M Paulsson
DOI: 10.1016/S0021-9258(18)47311-5
关键词:
摘要: Cartilage matrix protein (CMP), a major component of many types cartilage, is noncollagenous glycoprotein with molecular mass 148 kDa consisting three identical subunits. With the aim performing more comprehensive characterization, we purified CMP in native conformation from fetal bovine rib cartilage avoiding denaturing solvents previously used. could be selectively extracted EDTA-containing buffer which indicates divalent cation-dependent anchorage matrix. Determination amino-terminal sequence confirmed its identity when compared published cDNA sequences chicken and human CMP. Electron microscopy revealed presence ellipsoid subunits are connected at one end. Sequence analysis indicated coiled-coil alpha-helical assembly domain formed by COOH-terminal end The trimeric structure was retained after complete reduction under conditions shows that stable also absence interchain disulfide bonds.
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