Abstract:
:Binding of cefpiramide (CPM) and other beta-lactam antimicrobial agents to 2(3)-tert-butyl-4-hydroxyanisole (BHA)-induced liver glutathione (GSH) S-transferases (EC 2.5.1.18) from CD-1 mice was studied. A marked induction of hepatic GSH S-transferase from mice fed BHA was observed. Gel chromatography of liver cytosol from mice fed BHA showed an increased binding of CPM, cefotetan and cefazolin to BHA-induced GSH S-transferases. The extent of their binding to GSH S-transferase seemed to be correlated with the extent of their excretion into the bile. Binding of CPM to the GSH S-transferase fraction was inhibited by both indocyanine green, which is known to bind liver GSH S-transferases intensively, and by cefoperazon, which is mainly excreted into the bile. This study suggests that GSH S-transferases are the main binding proteins of CPM in the liver cytosol fraction and play an important role as carrier proteins of CPM and some antimicrobial agents in mouse liver.
journal_name
Pharmacologyjournal_title
Pharmacologyauthors
Nishiya H,Haga T,Nozue N,Komatsu T,Baba M,Ueda Y,Ono Y,Kunii Odoi
10.1159/000138600subject
Has Abstractpub_date
1989-01-01 00:00:00pages
213-23issue
4eissn
0031-7012issn
1423-0313journal_volume
39pub_type
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