Grigorovich Iu A, Bulgadaeva S A
Vopr Med Khim. 1986 May-Jun;32(3):36-41.
Activities of cyclic nucleotide phosphodiesterases (PDE) were studied in partially purified preparations from bovine and rabbit heart tissues. The PDE activity from rabbit heart was not increased in the course of purification and remained distinctly lower as compared with the enzymatic activity from bovine heart. Specific chelating agent Ca2+-EGTA (5 X 10(-4)M) inhibited effectively the PDE activity from bovine heart both in the ammonium sulfate fraction and in the fractions obtained by means of gel filtration on Sepharose 6B, but affected only slightly the enzyme activity from rabbit heart. The enzyme from bovine heart appears to involve mainly the Ca2+-calmodulin -dependent form, while the enzyme from rabbit heart, isolated under similar conditions, was Ca2+-calmodulin -independent. Phenothiazine derivatives inhibited distinctly the PDE activity from bovine heart at 5 X 10(-5)M concentration, whereas they did not affect or affected only slightly the enzyme preparations from rabbit heart even at 1 X 10(-4)M concentration; the inhibition was of the calmodulin -unspecific type. Phenothiazine derivatives (inhibitors of the calmodulin activity) exhibited only slight effect on the Ca2+-calmodulin -independent PDE from rabbit heart. This enzyme could not be used in studies of drugs, the effect of which is realized via regulation of the enzymatic activity by means of Ca2+ and calmodulin.
对牛和兔心脏组织部分纯化制剂中的环核苷酸磷酸二酯酶（PDE）活性进行了研究。兔心脏的PDE活性在纯化过程中未增加，与牛心脏的酶活性相比仍明显较低。特异性螯合剂Ca2+-EGTA（5×10（-4）M）有效抑制了牛心脏在硫酸铵级分以及通过Sepharose 6B凝胶过滤获得的级分中的PDE活性，但对兔心脏的酶活性影响很小。牛心脏的酶似乎主要涉及Ca2+-钙调蛋白依赖性形式，而在类似条件下分离的兔心脏的酶则不依赖于Ca2+-钙调蛋白。吩噻嗪衍生物在5×10（-5）M浓度下明显抑制牛心脏的PDE活性，而即使在1×10（-4）M浓度下，它们对兔心脏的酶制剂也没有影响或影响很小；这种抑制属于钙调蛋白非特异性类型。吩噻嗪衍生物（钙调蛋白活性抑制剂）对兔心脏中不依赖于Ca2+-钙调蛋白的PDE仅表现出轻微影响。这种酶不能用于研究那些通过Ca2+和钙调蛋白调节酶活性来实现其作用的药物。
