Abstract
Human renal dipeptidase (RDPase) was purified from surgically removed kidneys of renal stone patients by affinity chromatography using its specific inhibitor, cilastatin, as the ligand. The partial purified RDPase of 6 mg exhibited specific activity of 99.4 unit/mg with 2,029 fold purification. It was composed of a slow moving major band (96%) and a fast moving minor band (4%). The minor band was not a contaminant as it showed a dipeptidase-specific activity. The kinetic parameters determined with glycyldehydrophenylalanine (Gdp) as synthetic substrate were Vmax, 322.6 μmol/min/mg and Km, 0.102 mM. This experiment provided biochemical evidences that surgically removed, nonfunctional kidneys in respect of glomerular filtration still retained high activity of renal dipeptidase.
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Park, H.S., Kim, D.H., Kwark, H.S.E. et al. Human renal dipeptidase from kidneys of renal stone patients: Partial purification. Arch. Pharm. Res. 16, 295–299 (1993). https://doi.org/10.1007/BF02977519
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DOI: https://doi.org/10.1007/BF02977519