In vivo effect of chloramphenicol and thiamphenicol on some enzymes of normal mouse liver

Biochem Pharmacol. 1982 Jan 1;31(1):55-7. doi: 10.1016/0006-2952(82)90235-0.

Abstract

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.

MeSH terms

  • Animals
  • Chloramphenicol / pharmacology*
  • Enzyme Activation / drug effects
  • Glucuronidase / antagonists & inhibitors
  • Hydrolases / antagonists & inhibitors
  • Kynurenine / antagonists & inhibitors
  • Liver / enzymology*
  • Lyases*
  • Mice
  • Pyridoxal Kinase / metabolism
  • Pyruvates
  • Thiamphenicol / pharmacology*
  • Transaminases / antagonists & inhibitors

Substances

  • Pyruvates
  • Kynurenine
  • Chloramphenicol
  • Transaminases
  • glutamine - phenylpyruvate transaminase
  • kynurenine-oxoglutarate transaminase
  • Pyridoxal Kinase
  • Hydrolases
  • Glucuronidase
  • kynureninase
  • Lyases
  • Thiamphenicol