Monneron A, Ladant D, d'Alayer J, Bellalou J, Bârzu O, Ullmann A
Département de Biologie Moléculaire, Institut Pasteur, Paris, France.
Biochemistry. 1988 Jan 26;27(2):536-9. doi: 10.1021/bi00402a005.
A prokaryotic adenylyl cyclase, secreted by Bordetella pertussis, shares a common functional property with eukaryotic adenylyl cyclases, i.e., regulation by the eukaryotic protein calmodulin. Making use of polyclonal antibodies raised against the bacterial adenylyl cyclase and the rat brain adenylyl cyclase catalytic component, respectively, we showed an immunological cross-reactivity between the two enzymes. Furthermore, B. pertussis adenylyl cyclase was inhibited and immunoprecipitated by the homologous and one of the heterologous immune sera. These results suggest an evolutionary relationship between the B. pertussis enzyme and its eukaryotic counterpart.
百日咳博德特氏菌分泌的一种原核腺苷酸环化酶与真核腺苷酸环化酶具有共同的功能特性,即受真核蛋白钙调蛋白调节。分别利用针对细菌腺苷酸环化酶和大鼠脑腺苷酸环化酶催化成分产生的多克隆抗体,我们展示了这两种酶之间的免疫交叉反应性。此外,百日咳博德特氏菌腺苷酸环化酶被同源和一种异源免疫血清抑制并免疫沉淀。这些结果表明百日咳博德特氏菌的这种酶与其真核对应物之间存在进化关系。