VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

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

   
Isakhanian G.D., Gorkin V.Z.
PubMed Id: 7281562
Year: 1981  Volume: 27  Issue: 2  Pages: 228-235
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 length of the interval from composing the samples to monitoring the enzymatic activity and the following parameters of the AMP-deaminase: (a) shape of curves describing the rate of AMP deamination as a function of the nucleotide concentration, (b) reversible decrease in the AMP-deaminating activity after dialysis, (c) properties to deaminate, besides AMP, also some other nucleotides (ADP, NAD, FAD), (d) dynamics of inactivation of the enzyme preparations by controlled heating. The properties of the partially purified AMP-deaminase from the subfraction of rat liver soluble mitochondrial proteins were not identical with those described previously for other AMP-deaminases.
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Isakhanian, G. D., Gorkin, V. Z. (1981). Partial purification and properties of the adenylate deaminase from subfractions of soluble mitochondrial proteins of rat liver. Voprosy Meditsinskoi Khimii, 27(2), 228-235.
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