Lushchak V I, Storey K B
Biokhimiia. 1995 Feb;60(2):270-7.
AMP-deaminase was purified from trout white muscle and some of its properties were investigated. The enzyme preparation was electrophoretically homogeneous; the molecular mass of the polypeptides was equal to 71600 +/- 550 Da, the specific activity was 200-500 U./mg of protein. Activation of the enzyme caused by acidification of the medium in the physiological range of pH was the result of reduction of Km for the substrate. ADP and ATP activated the enzyme, while GTP inhibited it. The enzyme was also inhibited by IMP (this phenomenon had never been described before). A change in pH within the physiological range of pH (6.6-7.3) had no influence on ATP, GTP or IMP effects on AMP-deaminase. The enzyme activation by ADP was sensitive to pH. The possibilities of fish muscle AMP-deaminase regulation under conditions of intensified metabolism is discussed.
从鳟鱼白肌中纯化出腺苷酸脱氨酶，并对其一些特性进行了研究。该酶制剂在电泳上是均一的；多肽的分子量等于71600±550道尔顿，比活性为200 - 500单位/毫克蛋白质。在生理pH范围内，介质酸化引起的酶激活是底物Km降低的结果。ADP和ATP激活该酶，而GTP抑制它。该酶也被IMP抑制（这种现象以前从未被描述过）。在生理pH范围（6.6 - 7.3）内pH的变化对ATP、GTP或IMP对腺苷酸脱氨酶的作用没有影响。ADP对酶的激活对pH敏感。讨论了在代谢增强条件下鱼类肌肉腺苷酸脱氨酶的调节可能性。
