Molecular forms of human heart muscle AMP deaminase

¹Department of Biochemistry, Academic Medical School, Gdańsk, Poland.

Biochemical Medicine and Metabolic Biology

|October 1, 1991

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.

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