Kinetic studies of chloride inhibition in aspartate aminotransferase activity

Biochimie. 1989 Apr;71(4):417-25. doi: 10.1016/0300-9084(89)90172-7.

Abstract

The inhibitive effects of chloride anion on the activity of mitochondrial aspartate aminotransferase (L-aspartate: 2-oxoglutarate-aminotransferase EC. 2.6.1.1.) from chicken (Gallus domesticus) and turkey (Maleagris gallopavo) were studied. Steady-state velocities were obtained from a wide range of chloride concentrations. The data were fitted by rational functions of 0:2 and 1:2 for chloride, using a non-linear regression program which guaranteed the fit. The goodness of fit was improved by the use of a computer program that combined model discrimination, parameter refinement and sequential design. It was concluded that chloride aspartate aminotransferase inhibition requires a minimum velocity equation of 1:2 with regard to chloride, and a plausible kinetic mechanism for this experimental result was proposed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspartate Aminotransferases / antagonists & inhibitors
  • Aspartate Aminotransferases / metabolism*
  • Aspartic Acid / metabolism
  • Chickens
  • Chlorides / pharmacology*
  • Electronic Data Processing
  • In Vitro Techniques
  • Ketoglutaric Acids / metabolism
  • Kinetics
  • Mathematics
  • Mitochondria, Liver / enzymology
  • Models, Chemical
  • Turkeys

Substances

  • Chlorides
  • Ketoglutaric Acids
  • Aspartic Acid
  • Aspartate Aminotransferases