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뇨중 Urinary Dipeptidase 의 근원에 대한 고찰
박행순,김도하,박성광,강성귀,Marlyn Burks,James M . Mullins,Benedict J . Campbell ( Haeng Soon Park,Doh Ha Kim,Sung Kwang Park,Sung Kyew Kang,Marlyn Burks,James M . Mullins,Benedict J . Campbell ) 생화학분자생물학회 1992 BMB Reports Vol.25 No.4
Urinary dipeptidase, an enzyme with β-lactamase activity, was purified from the urine of healthy individuals. The purified enzyme was monophoretic when examined in polyacrylamide gel electrophoresis at pH 8.3, and its molecular mass estimated by HPLC was 227,000 daltons. It catalyzed the hydrolysis of the β-lactam antibiotic, N-formimidoyl-thienamycin (imipenem) with K_m=15.8 mM and V_(max)= 55 μ㏖/min/㎎. Lineweaver-Burk analysis of urinary dipeptidase-catalyzed hydrclysis of imipenem in the presence of cilastatin (Z-S-[6-carboxy-6-{ [2,2-dimethyl-(S)-cyclopropyl carboxy]-amino}-5-hexenyl]-L-cysteine) demonstrated reversible, competitive inhibition. The K_i for the competitive inhibitor, cilastatin, was 6 M. Renal dipeptidase was solubilized with n-butanol from membranes prepared from the kidneys of renal stone patients and purified. The two enzymes showed many properties in common including molecular mass, substrate specificity, kinetic parameters, inhibition by cilastatin, pH optima, electrophoretic mobility, and immunological cross-reactivity. Disintegration of kidney tubules and release of peptidase activity into the urine of rabbits treated with sublethal levels of the nephrotoxic agent, cephaloridine, suggest that the urinary dipeptidase originates from the proximal tubules of mammalian kidneys.