[Comparative characterization of catalytic properties of mitochondrial and cytoplasmic forms of NAD-dependent malate dehydrogenase from the rat liver at norm and in toxic hepatitis].

Abstract

The purification and comparative characterization of some catalytic properties of liver mitochondrial and cytosolic NAD-dependent malate dehydrogenase (NAD-MDH; EC 1.1.1.37) from normal rats and rats with experimental toxic hepatitis (ETH) have been carried out. It has been found that there are some differences in catalytic and regulatory properties of liver NAD-MDH from control animals and rats with ETH. It has been shown that Fe2+ and Cu2+ ions inhibit the enzyme, and the inhibition degree is different at norm and under toxic hepatitis. Ca2+ ions insignificantly activate cytosolic NAD-MDH under pathology and do not influence the mitochondrial isoform.

• Authors: E V Mikhaĭlova, T N Popova, O A Safonova
• Journal: Biomeditsinskaia khimiia (Biomed Khim) 2009 Jul-Aug Vol. 55 Issue 4 Pg. 489-99 ISSN: 2310-6972 [Print] Russia (Federation)
• PMID: 20000126 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Cations, Divalent
• Oxaloacetic Acid
• Copper
• Iron
• Malate Dehydrogenase
• Calcium

Topics

• Animals
• Calcium (chemistry)
• Catalysis
• Cations, Divalent
• Chemical and Drug Induced Liver Injury (enzymology)
• Copper (chemistry)
• Cytoplasm (enzymology)
• Enzyme Activation
• Hydrogen-Ion Concentration
• Iron (chemistry)
• Kinetics
• Liver (enzymology)
• Malate Dehydrogenase (antagonists & inhibitors, chemistry, isolation & purification)
• Male
• Mitochondria, Liver (enzymology)
• Oxaloacetic Acid (chemistry)
• Rats