title: Molecular forms of human heart muscle AMP deaminase.
abstract: Chromatography on phosphocellulose revealed the presence of two, kinetically different forms of human heart AMP deaminase. The main portion of the activity eluted from the column at about 1.1 M KCl, and the enzyme present in this eluate manifested a sigmoidal type of substrate saturation kinetics. The results from gel filtration indicate that human heart AMP deaminase is a tetrameric protein capable of aggregating in more complex active structures.
authors.affiliation: Department of Biochemistry, Academic Medical School, Gdańsk, Poland.
authors.forename: G
authors.initials: G
authors.lastname: Nowak
authors.forename: K
authors.initials: K
authors.lastname: Kaletha
mesh_terms: D000659:AMP Deaminase / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology*
chemical_list: D046911:Macromolecular Substances; D000659:AMP Deaminase