[Partial purification and properties of the adenylate deaminase from subfractions of soluble mitochondrial proteins of rat liver].

@article{Isakhanian1981PartialPA,
  title={[Partial purification and properties of the adenylate deaminase from subfractions of soluble mitochondrial proteins of rat liver].},
  author={G D Isakhanian and Vladimir Z. Gorkin},
  journal={Voprosy meditsinskoi khimii},
  year={1981},
  volume={27 2},
  pages={
          228-35
        }
}
Isolation and partial purification of AMP-deaminase from subfraction of soluble proteins of the mitochondrial fraction from rat liver is described. The enzyme preparations obtained deaminated AMP at the highest rate from pH 6.4 to 6.6. At the optimal pH value and in presence of optimal AMP concentrations the AMP-deaminase preparation was not activated by ATP or K+ and was inhibited by inorganic phosphate. Relationship was noted between both the content of protein in the enzyme preparations and… CONTINUE READING