Human Renal Dipeptidase from Kidneys of Renal Stone Patients: Partial Characterization

  • Park, Haeng-Soon (College of Pharmacy, Chonnam National University) ;
  • Kim, Doh-Ha (College of Pharmacy, Chonnam National University) ;
  • Kwark, Hyung S.Ellen (Pathology Department, Westchester County Medical Center) ;
  • Park, Sung-Kwang (Department of Internal Medicine, Chonbuk National University) ;
  • Kang, Sung-Kyew (Department of Internal Medicine, Chonbuk National University)
  • Published : 1994.02.01

Abstract

Physico-chemical characterization of human renal dipeptidase was carried out. It was a glycoprotein with a subunit MW of approximately 47,700 dalton. The pH optimum was at 8 and its stable conformation was retained between pH 5 and 12. The kinetic parameters determined with imipenem, a noval ${\beta}-lactam$ antibiotic, were Vmax, $5.21\;\mu{mol/min/mg}$; km, 4.35 mM ; and Ki with cilastatin, $0.25\;\mu{M}$ Cilastatin demonstrated reversible competitive inhibition.

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