The interaction of polyphosphoinositols with AMP deaminase.
Polyphosphoinositols coupled to epoxy-activated Sepharose retained chicken liver AMP deaminase in a similar manner as phosphocellulose. After elution from polyphosphoinositol-Sepharose, in contrast to inositol-Sepharose and phosphocellulose, low Km AMP deaminase from the chicken liver exhibited markedly elevated S0.5 value. Several commercially available polyphosphoinositols were tested with rat liver AMP deaminase and only 1,3,4,5 IP4 was found to stimulate the enzyme. This is the first report on the effect of naturally occurring polyphosphoinositol derivative on the soluble enzyme.
Spychała
J
J
Department of Biochemistry, Academic Medical School, Gdańsk, Poland.
D000659:AMP Deaminase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D007295:Inositol Phosphates / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009709:Nucleotide Deaminases / Q000378:metabolism*; D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols / Q000378:metabolism*; D012685:Sepharose
D007295:Inositol Phosphates; D018129:Phosphatidylinositol Phosphates; D010716:Phosphatidylinositols; D012685:Sepharose; D009709:Nucleotide Deaminases; D000659:AMP Deaminase