Partial characterization of microsomal sialyltransferase from chicken liver and hepatoma Mc-29: I. Effect of nucleotides and metal ions.

Abstract

CMP-N-acetylneuraminic acid: glycoprotein sialyltransferase activities were assayed in microsomal fractions from chicken liver and hepatoma, induced by the leukosis virus strain Mc-29, using asialofetuin as the substrate acceptor of N-acetylneuraminic acid. The effect of some nucleotides and metal ions on the enzyme activity was investigated. Kinetic studies revealed that the Km values toward asialofetuin at a saturation concentrations of CMP-N-acetylneuraminic acid for both liver and hepatoma enzymes are very closed, while V value was lower for the tumor enzyme. The liver and hepatoma enzymes have no exogenous Mn cations requirement and are inhibited by CTP, CMP and ATP. CMP was shown to act as a competitive inhibitor with an apparent Ki of 0.24 mM for the liver and 0.16 mM for hepatoma enzyme, respectively.

• Authors: V K Karaivanova, S X Ivanov, H Chelibonova-Lorer
• Journal: Cancer biochemistry biophysics (Cancer Biochem Biophys) Vol. 11 Issue 4 Pg. 303-10 (Nov 1990) ISSN: 0305-7232 [Print] England
• PMID: 2081338 (Publication Type: Journal Article)

Chemical References

• Ribonucleotides
• Manganese
• Sialyltransferases
• Magnesium

Topics

• Animals
• Chickens
• Kinetics
• Liver Neoplasms, Experimental (enzymology)
• Magnesium (pharmacology)
• Manganese (pharmacology)
• Microsomes (enzymology)
• Microsomes, Liver (enzymology)
• Ribonucleotides (pharmacology)
• Sialyltransferases (metabolism)