PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15764716-6 2005 Hepatocytes that contain both dihydropyrimidinase and dihydroorotase completely hydrolyzed dexrazoxane to ADR-925 and released it into the extracellular medium. Dexrazoxane 91-102 dihydropyrimidinase Rattus norvegicus 30-49 7900413-4 1994 4-Chlorobenzenesulphonamide, which is a strong inhibitor of dihydropyrimidine amidohydrolase (DHPase), caused 82% inhibition of the loss of dexrazoxane from the hepatocyte suspension. Dexrazoxane 154-165 dihydropyrimidinase Rattus norvegicus 74-106 7900413-4 1994 4-Chlorobenzenesulphonamide, which is a strong inhibitor of dihydropyrimidine amidohydrolase (DHPase), caused 82% inhibition of the loss of dexrazoxane from the hepatocyte suspension. Dexrazoxane 154-165 dihydropyrimidinase Rattus norvegicus 108-114 7900413-9 1994 The ratios of the rates at which each of the one-ring open intermediates of dexrazoxane and levrazoxane were produced in the hepatocyte suspension are also consistent with DHPase being primarily responsible for the metabolism of dexrazoxane and levrazoxane. Dexrazoxane 76-87 dihydropyrimidinase Rattus norvegicus 172-178 7900413-9 1994 The ratios of the rates at which each of the one-ring open intermediates of dexrazoxane and levrazoxane were produced in the hepatocyte suspension are also consistent with DHPase being primarily responsible for the metabolism of dexrazoxane and levrazoxane. Dexrazoxane 229-240 dihydropyrimidinase Rattus norvegicus 172-178 7900413-11 1994 Thus, the DHPase-catalysed formation of the one-ring opened intermediates enhances the rate at which the presumably active metal-ion binding forms of dexrazoxane are produced in the hepatocyte. Dexrazoxane 150-161 dihydropyrimidinase Rattus norvegicus 10-16