Hewlett E L, Underhill L H, Cook G H, Manclark C R, Wolff J
J Biol Chem. 1979 Jul 10;254(13):5602-5.
The activity of Bordetella pertussis extracytoplasmic adenylate cyclase is 100-fold higher in organisms grown on blood agar than in those grown in synthetic medium. This increase in activity is due to in vivo activation of the enzyme by a factor present in erythrocytes. Activation also occurs in killed or disrupted organisms. The activator can be separated from heme proteins and has been purified approximately 100-fold from erythrocytes, yielding material of approximately 105,000 daltons. It is sensitive to trypsin and alpha-chymotrypsin and exhibits considerable heat stability. Activation of cyclase in intact B. pertussis organisms exhibits a lag of 3 to 4 min and is not reversed by washing. Response to the activator decreases with increasing purification of the adenylate cyclase and is absent in the pure enzyme. The activation does not appear to be proteolytic and does not appear to change access to the substrate, ATP. The activator has no effect on a number of eukaryotic cyclases. We conclude that this is a new type of activation and that the activator differs from all those previously described.
百日咳博德特氏菌胞外腺苷酸环化酶在血琼脂上生长的菌体中的活性，比在合成培养基中生长的菌体高100倍。活性的这种增加是由于该酶在体内被红细胞中存在的一种因子激活。在杀死的或破碎的菌体中也会发生激活。激活剂可以与血红素蛋白分离，并且已从红细胞中纯化了约100倍，得到分子量约为105,000道尔顿的物质。它对胰蛋白酶和α-糜蛋白酶敏感，并表现出相当的热稳定性。完整的百日咳博德特氏菌菌体中环化酶的激活表现出3至4分钟的延迟，并且洗涤后不会逆转。随着腺苷酸环化酶纯化程度的提高，对激活剂的反应降低，纯酶中不存在这种反应。这种激活似乎不是蛋白水解作用，也似乎不会改变对底物ATP的利用。该激活剂对多种真核环化酶没有影响。我们得出结论，这是一种新型的激活作用，并且该激活剂与先前描述的所有激活剂都不同。
