title: Purification and general properties of AMP deaminase from sheep brain.
abstract: AMP deaminase from sheep brain was purified to homogeneity on SDS-PAGE and its general properties were investigated. The native enzyme has a molecular weight of approximately 350,000 as estimated by gel filtration and it is composed of four identical subunits with a molecular weight of 85,000 each. The purified enzyme had a specific activity of 500 units/mg protein and shows a sigmoid-shaped AMP saturation curve in the presence of 100 mM KCl. This deaminase is strongly activated by ATP and inhibited by GTP. It slightly catalyzes the hydrolysis of adenosine monosulfate (AMS), dAMP, and adenosine phosphoramidate (APA). These catalytic properties resemble those of AMP deaminase from human liver.
authors: Department of Pharmaceutical Sciences, Tohoku University Hospital, Miyagi.
authors: K
authors: K
authors: Ito
authors: H
authors: H
authors: Yamamoto
authors: M
authors: M
authors: Mizugaki
mesh_terms: D000659:AMP Deaminase / Q000032:analysis / Q000302:isolation & purification*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000032:analysis / Q000302:isolation & purification*; D007700:Kinetics; D008970:Molecular Weight; D009709:Nucleotide Deaminases / Q000302:isolation & purification*; D012756:Sheep; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D009709:Nucleotide Deaminases; D000659:AMP Deaminase