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人类红细胞腺苷酸激酶两种常见遗传形式的部分纯化及特性

Partial purification and properties of the two common inherited forms of human erythrocyte adenylate kinase.

作者信息

Brownson C, Spencer N

出版信息

Biochem J. 1972 Dec;130(3):797-803. doi: 10.1042/bj1300797.

Abstract
  1. The partial purification of adenylate kinase, types 1 and 2, from human erythrocytes is described. 2. Gel chromatography of both forms of the enzyme gave estimates of the molecular weights in the range 20000-23000. 3. Studies on crude haemolysates at various pH values indicated that the type 2 enzyme was less stable than the type 1. Heat denaturation studies on the partially purified enzymes confirmed these findings. 4. Measurements of rates of inhibition by iodoacetate and iodoacetamide showed that the type 2 enzyme reacts more readily than the type 1 enzyme with both reagents. 5. The effect of temperature on the initial velocity of ADP formation was measured at a single concentration of both AMP and MgATP(2-). The two forms of the enzyme responded differently to increasing temperature.
摘要
  1. 描述了从人红细胞中对1型和2型腺苷酸激酶的部分纯化。2. 对两种形式的酶进行凝胶色谱分析,得出分子量估计值在20000 - 23000范围内。3. 在不同pH值下对粗溶血产物的研究表明,2型酶比1型酶更不稳定。对部分纯化酶的热变性研究证实了这些发现。4. 对碘乙酸盐和碘乙酰胺抑制率的测量表明,2型酶与这两种试剂的反应比1型酶更迅速。5. 在AMP和MgATP(2-)的单一浓度下,测量了温度对ADP形成初始速度的影响。两种形式的酶对温度升高的反应不同。

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