AMP deaminase from the gill of the mullet Chelon labrosus R.: purification and effects of pH, phosphate and monovalent cations.
The AMP deaminase from the gill of Chelon labrosus was purified about 250-fold by chromatography on cellulose-phosphate. At low and high substrate concentration, a sharp pH optimum was found between pH 6.7 and 6.9. The enzyme was found to be relatively insensitive to physiological concentrations of inorganic phosphate. Na+ and K+ were activators of gill AMP deaminase, Na+ being the most efficient. Effects of possible changes in the intracellular concentrations of these cations on enzyme activity are discussed.
D000659:AMP Deaminase / Q000302:isolation & purification*; D000818:Animals; D002414:Cations, Monovalent; D004789:Enzyme Activation / Q000187:drug effects; D005399:Fishes / Q000378:metabolism*; D005880:Gills / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D009709:Nucleotide Deaminases / Q000302:isolation & purification*; D010710:Phosphates / Q000494:pharmacology*; D011188:Potassium / Q000494:pharmacology; D012964:Sodium / Q000494:pharmacology; D013045:Species Specificity
D002414:Cations, Monovalent; D010710:Phosphates; D012964:Sodium; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D011188:Potassium