Abstract
Several proteinase activities associated with different molecular weight proteins were detected by substrate-gel electrophoresis using gelatin as a substrate in the 4M guanidine soluble fraction obtained from the demineralized matrix of the mineralized phase of newborn rat calvaria (mineralized phase matrix proteinases = MPM proteinases). The major gelatinase activity migrated with the molecular weight fraction of 58,000 daltons. This proteinase was active over the pH range 6–9 against gelatin. Based on the behavior against inhibitors and the differences of molecular weight, the 58kD MPM proteinase was thought to be different from the already known matrix metalloproteinases and proteinases such as kallikrain, plasmin and cathepsin B 1. Some of bone MPM proteinases may participate in the degradation of acidic proteins (sialoprotein and phosphorylated proteins) which are stained blue with Stains-all in newborn rat calvaria.
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Fukae, M., Tanabe, T. & Yamada, M. Mineralized phase matrix proteinases of newborn rat calvaria. J Bone Miner Metab 8, 12–18 (1990). https://doi.org/10.1007/BF02377368
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DOI: https://doi.org/10.1007/BF02377368