In vivo effect of chloramphenicol and thiamphenicol on some enzymes of normal mouse liver.
Chloramphenicol a potent inhibitor of bacterial and some mammalian cell protein synthesis, was administered i.p. to a group of mice for 6 consecutive days. Another group of animals was treated similarly with thiamphenicol and a third group served as control. The effects of the two antibiotics on the activity of some liver enzymes; the two pyridoxal 5-phosphate dependent enzymes, kynurenine hydrolase and kynurenine amino-transferase; pyridoxal phosphokinase; beta-glucuronidase and acid ribonuclease were determined. Chloramphenicol and thiamphenicol decreased significantly the activities of kynurenine hydrolase, beta-glucuronidase and acid ribonuclease and both drugs increased the activity of pyridoxal phosphokinase significantly. Their effect on kynurenine amino-transferase was different, chloramphenicol decreased while thiamphenicol increased the enzyme activity. Results are discussed and possible explanations suggested.
D000818:Animals; D002701:Chloramphenicol / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D005966:Glucuronidase / Q000037:antagonists & inhibitors; D006867:Hydrolases / Q000037:antagonists & inhibitors; D007737:Kynurenine / Q000037:antagonists & inhibitors; D008099:Liver / Q000201:enzymology*; D008190:Lyases; D051379:Mice; D011731:Pyridoxal Kinase / Q000378:metabolism; D011773:Pyruvates; D013839:Thiamphenicol / Q000494:pharmacology*; D000637:Transaminases / Q000037:antagonists & inhibitors
D011773:Pyruvates; D007737:Kynurenine; D002701:Chloramphenicol; D000637:Transaminases; C427605:glutamine - phenylpyruvate transaminase; C021481:kynurenine-oxoglutarate transaminase; D011731:Pyridoxal Kinase; D006867:Hydrolases; D005966:Glucuronidase; C021480:kynureninase; D008190:Lyases; D013839:Thiamphenicol