Direct Deamination of Adenosine Diphosphate by Washed Myofibrils

Abstract

THE deamination of adenine nucleotides homogenates and extracts of skeletal muscle is usually ascribed to the action of an enzyme, originally described by Schmidt¹, which specifically deaminates adenosine monophosphate. Direct deamination of adenosine triphosphate has not been demonstrated, though the work of Banga and Josepovits² suggested a simultaneous production of inorganic phosphate and ammonia from adenosine diphosphate. This effect required the presence of myosin plus a ‘protin’ preparation, and an isomer of adenosine diphosphate was postulated as an intermediate compound. This claim has been criticized adversely by Bailey³.