Purification and characterization of diphosphopyridine nucleosidase from pig brain.

摘要: Abstract Particulate diphosphopyridine nucleosidase from pig brain has been solubilized with trypsin and purified 8000-fold. The material appeared to be homogeneous in the ultracentrifuge; an s20,w value of 2.5 a molecular weight 26,000 were derived for enzyme. protein gave one precipitin band, indicative species antigen, specific rabbit antibody. Less than 5% contaminant was present as determined by cellulose acetate electrophoresis. Amino acid composition enzyme differed significantly that Bacillus subtilis nucleosidase. acetone powder exhibited identical catalytic properties respect hydrolysis nucleotide, 3-acetylpyridine exchange, specificity DPN+ TPN+, well pH profiles. trypsin-solubilized enzyme, lipase, had weights 25,000 (±1,000), respectively, on Sephadex G-100. Both forms same electrophoretic mobility staining technique developed test mammalian nucleosidases. These results indicate possesses solubilization does not alter native since it is lipase-solubilized material.