Ofulue A F, Nijjar M S
Biochem J. 1981 Dec 15;200(3):475-80. doi: 10.1042/bj2000475.
Adenylate cyclase activity in the rat lung membranes washed with 150 microM-EGTA was stimulated by calmodulin in the presence of 100 microM-Ca2+. The calmodulin activation of the enzyme was concentration-dependent; however, at high concentrations the activation was diminished. Activation of adenylate cyclase by calmodulin was immediate, reversible and due to an increase in the Vmax. without apparent effect on the affinity of the enzyme for ATP. The rat lung supernatant produced additive activation of the adenylate cyclase that was already maximally stimulated by calmodulin, indicating that either calmodulin and cytoplasmic factors act at different sites on adenylate cyclase or different adenylate cyclases may be involved. The data further support our previous conclusion that calmodulin is not involved in the activation of adenylate cyclase by cytoplasmic factors in rat lungs.
用150微摩尔乙二醇双(2-氨基乙基醚)四乙酸(EGTA)洗涤的大鼠肺膜中的腺苷酸环化酶活性,在存在100微摩尔钙离子(Ca2+)的情况下受到钙调蛋白的刺激。钙调蛋白对该酶的激活呈浓度依赖性;然而,在高浓度时激活作用减弱。钙调蛋白对腺苷酸环化酶的激活是即时的、可逆的,并且是由于最大反应速度(Vmax)增加,而对该酶与三磷酸腺苷(ATP)的亲和力没有明显影响。大鼠肺上清液对已经被钙调蛋白最大程度刺激的腺苷酸环化酶产生加性激活,这表明要么钙调蛋白和细胞质因子作用于腺苷酸环化酶的不同位点,要么可能涉及不同的腺苷酸环化酶。这些数据进一步支持了我们之前的结论,即钙调蛋白不参与大鼠肺中细胞质因子对腺苷酸环化酶的激活。