Molecular forms of human heart muscle AMP deaminase.
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.
Nowak
G
G
Department of Biochemistry, Academic Medical School, Gdańsk, Poland.
Kaletha
K
K
D000659:AMP Deaminase / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology*
D046911:Macromolecular Substances; D000659:AMP Deaminase