Abstract
Meprin is a membrane-bound metallo-proteinase that is present in high concentrations in the kidney brush border of mice and rats (Bond and Beynon, 1986). The enzyme has been purified and found to exist as a tetrameric glycoprotein that contains one mol zinc and three mol calcium per 85,000 molecular weight subunit (Beynon et al., 1981; Butler et al., 1987). Meprin hydrolyzes a variety of peptide and protein substrates (e.g., insulin B chain, glucagon, angiotensins I and II, bradykinin, hemoglobin, casein, aldolase, and phosphorylase kinase); the substrate used most often to assay activity is azocasein, a good general substrate for neutral and alkaline proteinases.
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References
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© 1988 Plenum Press, New York
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Reckelhoff, J.F., Craig, S.S., Beynon, R.J., Bond, J.S. (1988). Meprin Phenotype and Cyclosporin A Toxicity in Mice. In: Hörl, W.H., Heidland, A. (eds) Proteases II. Advances in Experimental Medicine and Biology, vol 240. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1057-0_34
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DOI: https://doi.org/10.1007/978-1-4613-1057-0_34
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