Purification and properties of a nucleoside triphosphatase from Sinclair swine.

Abstract

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.

• Authors: M V Williams
• Journal: Enzyme (Enzyme) Vol. 32 Issue 4 Pg. 201-7 ( 1984) ISSN: 0013-9432 [Print] Switzerland
• PMID: 6098441 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Phosphoric Monoester Hydrolases
• Nucleoside-Triphosphatase

Topics

• Animals
• Kinetics
• Melanoma (enzymology)
• Nucleoside-Triphosphatase
• Phosphoric Monoester Hydrolases (antagonists & inhibitors, isolation & purification)
• Skin (enzymology)
• Skin Neoplasms (enzymology)
• Swine