Slinchenko N N, Shlykov S G, Kurskiĭ M D
Ukr Biokhim Zh (1978). 1982 May-Jun;54(3):259-63.
Some kinetic properties of adenylate cyclase of plasma membrane myometrium were studied in nonpregnant rabbit. The apparent Km for ATP and V were 0.38 mM and 125 pmol cAMP/mg protein/min, respectively. The maximal activity of enzyme was observed at the Mg2+ concentration of about 15-20 mM and pH 7.7-7.9. Adenylate cyclase possessed sensitivity for F-, the maximal stimulation was observed at the F- concentration of 15 mM. 2 mM EGTA, 10(-8) M Ca2+ activated the enzyme. Argumentation of the Ca2+ concentration from 10(-7) to 10(-3) M led to adenylate cyclase inhibition.
在未孕兔中研究了子宫肌层质膜腺苷酸环化酶的一些动力学特性。ATP的表观Km值和V分别为0.38 mM和125 pmol cAMP/毫克蛋白/分钟。在镁离子浓度约为15 - 20 mM和pH 7.7 - 7.9时观察到酶的最大活性。腺苷酸环化酶对氟离子敏感，在氟离子浓度为15 mM时观察到最大刺激作用。2 mM乙二醇双乙醚二胺四乙酸、10(-8) M钙离子激活该酶。将钙离子浓度从10(-7) M增加到10(-3) M会导致腺苷酸环化酶受到抑制。
