Ladant D, Brezin C, Alonso J M, Crenon I, Guiso N
J Biol Chem. 1986 Dec 5;261(34):16264-9.
The extracellular adenylate cyclase of Bordetella pertussis was purified either as a free enzyme or as a complex with calmodulin. The purified enzyme has a specific activity of 1600 mumol of cAMP min-1 X mg-1 and exists under two molecular forms of 45 and 43 kDa which are apparently structurally related. Calmodulin increased considerably the resistance of adenylate cyclase to inactivation by trypsin. Although trypsin cleaved the adenylate cyclase-calmodulin complex, the digested fragments remained associated by noncovalent interactions in an active conformation. Specific mouse anti-adenylate cyclase antibodies inhibit adenylate cyclase activity and were used to develop a specific radioimmunoassay that allows detection of as little as 5 ng of adenylate cyclase in culture supernatants.
百日咳博德特氏菌的细胞外腺苷酸环化酶可以作为游离酶或与钙调蛋白的复合物进行纯化。纯化后的酶具有1600 μmol cAMP min⁻¹·mg⁻¹的比活性，以45 kDa和43 kDa两种分子形式存在，这两种形式在结构上显然相关。钙调蛋白显著提高了腺苷酸环化酶对胰蛋白酶失活的抗性。虽然胰蛋白酶切割了腺苷酸环化酶 - 钙调蛋白复合物，但消化后的片段通过非共价相互作用以活性构象保持结合。特异性小鼠抗腺苷酸环化酶抗体抑制腺苷酸环化酶活性，并用于开发一种特异性放射免疫测定法，该方法能够检测培养上清液中低至5 ng的腺苷酸环化酶。
