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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Biochem J. 1967 Oct;105(1):279-88. doi: 10.1042/bj1050279.

The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0 degrees than at 25 degrees but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg(2+) or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg(2+)-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg(2+) activation indicate that the ATP-Mg(2+) complex is the important substrate: free ATP and Mg(2+) are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).

本文描述了从丙酮干燥的牛心线粒体水提取物中纯化一种三磷酸腺苷酶的方法。2. 未发现这些提取物中存在不止一种具有三磷酸腺苷酶活性的蛋白质。3. 该酶在0℃时比在25℃时更不稳定，但甘油可使其稳定。4. 活性依赖于Mg(2+)或某些其他二价金属阳离子的存在。5. 2,4-二硝基苯酚可增强Mg(2+)激活的酶的三磷酸腺苷酶活性。6. Mg(2+)激活的动力学表明ATP-Mg(2+)复合物是重要底物：游离的ATP和Mg(2+)具有抑制作用。7. 这种线粒体三磷酸腺苷酶制剂与线粒体的三磷酸腺苷酶偶联因子有许多共同特性（拉克尔，1961年）。

Biochem J. 1967 Oct;105(1):279-88. doi: 10.1042/bj1050279.

The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0 degrees than at 25 degrees but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg(2+) or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg(2+)-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg(2+) activation indicate that the ATP-Mg(2+) complex is the important substrate: free ATP and Mg(2+) are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).

本文描述了从丙酮干燥的牛心线粒体水提取物中纯化一种三磷酸腺苷酶的方法。2. 未发现这些提取物中存在不止一种具有三磷酸腺苷酶活性的蛋白质。3. 该酶在0℃时比在25℃时更不稳定，但甘油可使其稳定。4. 活性依赖于Mg(2+)或某些其他二价金属阳离子的存在。5. 2,4-二硝基苯酚可增强Mg(2+)激活的酶的三磷酸腺苷酶活性。6. Mg(2+)激活的动力学表明ATP-Mg(2+)复合物是重要底物：游离的ATP和Mg(2+)具有抑制作用。7. 这种线粒体三磷酸腺苷酶制剂与线粒体的三磷酸腺苷酶偶联因子有许多共同特性（拉克尔，1961年）。