Purification and properties of a nucleoside triphosphatase from Sinclair swine.

A nonspecific nucleoside triphosphatase was partially purified from skin and cutaneous melanoma tumors from Sinclair swine using chloroform precipitation, hydrophobic, ion-exchange and affinity chromatography techniques. The enzyme was not stimulated by Na+, K+ or Mg2+ but it was inhibited by EDTA. The enzyme was not inhibited by quercetin, proflavin, azide or ovabain. The enzyme exhibited optimal activity over a pH range of 8-9 and the activation energy was 10.4 and 9.8 kcal/mol for dUTP and ATP, respectively. The apparent Km of the enzyme for dUTP and dTTP was approximately 20 mumol/l while the apparent Km for dATP, ATP, dCTP, CTP and UTP was in the range of 65-80 mumol/l.