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1 From the Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee
The thermolabile, non dialysable inhibitor of d-amino acid oxidase has been further investigated.
It can be precipitated by half saturation with ammonium sulphate and by saturation with magnesium sulphate or sodium chloride.
Adsorption on and elution from cupric hydroxide increases the purity
The solubility properties indicate that it is a globulin like substance
Phosphate in high concentrations inhibits its activity
The activity is greater at low pH's than at high pH's
The combination with d-amino acid oxidase appears to be reversible since a decrease in inhibition is observed when the pH is raised.
Kinetic studies indicate that it does not compete with the coenzyme for the apoenzyme, neither does it compete with the substrate for the apoenzyme-coenzyme complex. It appears to form an apoenzyme-coenzyme-substrate-inhibitor complex.
Submitted on May 10, 1945