Purification of nucleoside phosphotransferase from mucosa of chicken intestine

Abstract

The authors describe the purification procedure and some properties of a nucleoside phosphotransferase obtained from chicken intestinal mucosa, the tissue of which in preliminary studies showed the highest specific activity. Sepharose 6B chromatography and electrophoresis on polyacrylamide gel subdivided the enzyme into many forms which represent various levels of an associated multisubunit protein derived by assembly of a component at lower molecular weight. Nucleotide protectors regulate the equilibrium among these different forms, favoring the production and the stabilization of supramolecular complexes of nucleoside phosphotransferase. Similar results were obtained with enzyme purified from brain, muscle and embryos of chicken by means of the procedure described.