Raffin J P
Comp Biochem Physiol B. 1984;79(3):499-504. doi: 10.1016/0305-0491(84)90412-7.
The AMP deaminase isoenzymes from trout gill were activated by sodium and potassium, sodium being the most efficient. The optimal concentration for activation was 30-50 mM. The enzyme was sensitive to ionic strength, and imidazole was an inhibitor at concentrations higher than 25 mM. A possible regulation of gill AMP deaminase by intracellular imidazole buffers is discussed. AMP deaminase activity was tested in the presence of physiological concentrations of sodium and potassium. When the concentration of one of these cations was varied around its physiological concentration, the enzyme activity was relatively stable, indicating that the intracellular AMP deaminase activity would be insensitive to changes in the concentrations of monovalent cations. The effects of the sodium salts of different inorganic and organic anions were tested. Except chloride and gluconate, all were inhibitors of gill AMP deaminase.
虹鳟鱼鳃中的AMP脱氨酶同工酶可被钠和钾激活，其中钠的激活效果最佳。激活的最佳浓度为30 - 50 mM。该酶对离子强度敏感，咪唑在浓度高于25 mM时为抑制剂。文中讨论了细胞内咪唑缓冲剂对鳃AMP脱氨酶的可能调节作用。在生理浓度的钠和钾存在下测试了AMP脱氨酶活性。当其中一种阳离子的浓度在其生理浓度附近变化时，酶活性相对稳定，这表明细胞内AMP脱氨酶活性对单价阳离子浓度的变化不敏感。测试了不同无机和有机阴离子钠盐的作用。除了氯离子和葡萄糖酸盐外，其他都是鳃AMP脱氨酶的抑制剂。
