作者:H. L. WEBSTER
DOI:10.1038/172453a0
日期:1953.9
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。