Meisel P, Meisel M, Grisk A
Cor Vasa. 1976;18(1):56-65.
Because of some uncertainties still existing about the role of adenosine deaminase in the drug-influenced adenosine breakdown, the authors isolated this enzyme from vascular smooth muscle and studied the inhibition of its activity by some vasodilating drugs. The adenosine deaminase was purified 360-fold from bovine carotid artery by means of (NH4)2SO4-precipitation, heat treatment, and gel filtration. This enzyme behaves in a similar way as preparations of the same enzyme from other tissues in respect to pH-dependence and Michaelis constant. The vascular enzyme is inhibited by dipyridamole and trapymine in a competitive manner, hexobendine and lidoflazine are without any effect. The results lead to the conclusion that the inhibition of vascular adenosine deaminase does not constitute the sole cause of the adenosine-potentiating effect of the vasodilating drugs studied.
由于腺苷脱氨酶在药物影响的腺苷分解过程中的作用仍存在一些不确定性，作者从血管平滑肌中分离出这种酶，并研究了一些血管舒张药物对其活性的抑制作用。通过硫酸铵沉淀、热处理和凝胶过滤，从牛颈动脉中纯化出360倍的腺苷脱氨酶。就pH依赖性和米氏常数而言，这种酶的行为与来自其他组织的相同酶制剂相似。血管酶受到双嘧达莫和曲匹明的竞争性抑制，己酮可可碱和利多氟嗪则无任何作用。结果得出结论，所研究的血管舒张药物的腺苷增强作用并非仅由血管腺苷脱氨酶的抑制所致。
