Studies on acylneuraminate cytidylytransferase from human placenta.
The presence of acylneuraminate cytidylyltransferase has not been shown in human placenta so far. In this paper, evidence is put forward to demonstrate the presence of this enzyme in human placenta. The soluble enzyme was partially purified 30-fold using ammonium sulphate fractionation (30-60%) and DEAE Sephadex A-50 chromatography. This enzyme preparation had a specific activity of 0.75 mkat/kg protein. The pH optimum of the reaction was 9.0. The Km values for N-acetylneuraminic acid and cytidine triphosphate were 2.2 mM and 4 mM respectively. It was also found that the presence of magnesium is necessary for the enzyme activity.
D002413:Cations, Divalent; D002845:Chromatography; D003570:Cytidine Triphosphate / Q000378:metabolism; D005260:Female; D006801:Humans; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D019158:N-Acetylneuraminic Acid; D000216:N-Acylneuraminate Cytidylyltransferase / Q000302:isolation & purification / Q000378:metabolism*; D009713:Nucleotidyltransferases / Q000378:metabolism*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D012794:Sialic Acids / Q000378:metabolism
D002413:Cations, Divalent; D012794:Sialic Acids; D003570:Cytidine Triphosphate; D009713:Nucleotidyltransferases; D000216:N-Acylneuraminate Cytidylyltransferase; D019158:N-Acetylneuraminic Acid; D008274:Magnesium