Mass action ratios of the adenylate kinase reaction

Range Table - link
Organism Rat Rattus norvegicus
Reference Soboll S, Scholz R, Heldt HW. Subcellular metabolite concentrations. Dependence of mitochondrial and cytosolic ATP systems on the metabolic state of perfused rat liver. Eur J Biochem. 1978 Jun 15 87(2):377-90. p.389 table 10PubMed ID668699
Method “From marker enzyme activities and metabolite contents in the unfractionated homogenate and in the different fractions the mitochondrial and cytosolic metabolite contents (nmol/mg protein) were calculated by extrapolating the data to fractions of pure mitochondria and pure cytosol according to Elbers et al. [ref 5]. The subcellular metabolite contents were converted into concentrations assuming a water content of 0.8 and 3.8 µl/mg protein in the mitochondrial and cytosolic compartment, respectively, based on considerations previously discussed by Soboll et al. [ref 1].”
Comments "The mass action ratios of the adenylate kinase reaction calculated from the cytosolic concentrations of ATP, ADP and AMP varied closely around 0.8 under all metabolic conditions (Table 10). This value is in the range of the equilibrium constants reported for isolated adenylate kinase [29- 31]. Apparently, in the cytosol the adenine nucleotides are in a near equilibrium catalyzed by the adenylate kinase. In the mitochondrial compartment, the mass action ratio is more than ten-times higher than in the cytosol. i.e. the AMP concentration found is much lower than to be expected under equilibrium conditions." For experimental conditions and metabolic states see p.381 table 1 link
Entered by Uri M
ID 111359