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 âprotinâ preparation, and an isomer of adenosine diphosphate was postulated as an intermediate compound. This claim has been criticized adversely by Bailey3.
腺嘌呤核苷酸匀浆和骨骼肌
提取物的脱
氨基通常归因于一种酶的作用,该酶最初由 Schmidt1 描述,该酶特异性地使单
磷酸腺苷脱
氨基。尽管 Banga 和 Josepovits2 的工作表明可以从
二磷酸腺苷同时生产无机
磷酸盐和
氨,但
三磷酸腺苷的直接脱
氨基尚未得到证实。这种效应需要肌球蛋白加“蛋白质”制剂的存在,并且
二磷酸腺苷异构体被假定为中间化合物。这一说法遭到贝利3的不利批评。