title: Inactivation of new carbapenem antibiotics by dehydropeptidase-I from porcine and human renal cortex.
abstract: The stability of the new carbapenem antibiotics, panipenem, meropenem and LJC 10,627, against porcine and human renal dehydropeptidase-I (DHP-I) was compared with that of imipenem. The order of stability to hydrolysis by renal DHP-I was: LJC 10,627 greater than meropenem greater than panipenem greater than imipenem. After incubation of the drugs with porcine or human enzyme at 30 degrees C for 4 h, the percentages of residual activity were as follows: LJC 10,627, 73.7% and 95.6%, respectively; meropenem, 0.2% and 28.7%, respectively; panipenem, 0% and 4.3%, respectively; and imipenem, 0% and 0.1%, respectively. These results demonstrate that LJC 10,627 has extremely high stability against renal DHP-I.
authors.affiliation: Episome Institute, Gunma, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Hikida
authors.forename: K
authors.initials: K
authors.lastname: Kawashima
authors.forename: M
authors.initials: M
authors.lastname: Yoshida
authors.forename: S
authors.initials: S
authors.lastname: Mitsuhashi
mesh_terms: D000818:Animals; D015780:Carbapenems / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D004150:Dipeptidases / Q000378:metabolism*; D006801:Humans; D015378:Imipenem / Q000494:pharmacology; D007672:Kidney Cortex / Q000201:enzymology*; D013552:Swine
chemical_list: D015780:Carbapenems; D015378:Imipenem; D004150:Dipeptidases; C038937:dipeptidase