Müller M, Labonia N, Azzi A
Institut für Biochemie und Molekularbiologie der Universität Bern, Switzerland.
Biochem Biophys Res Commun. 1988 Aug 15;154(3):1260-5. doi: 10.1016/0006-291x(88)90275-6.
Polyclonal antibodies have been obtained against a synthetic dodecapeptide identical to the aminoacid sequence 120-131 DSPIKDGVWPPE (inferred from its DNA sequence) of Paracoccus denitrificans cytochrome c oxidase subunit III. The antibodies had a titer higher than 1:10000 when tested against the antigen. These antibodies have been used to produce immunological evidence that, despite the fact that subunit III is not isolated with cytochrome c oxidase, it exists in Paracoccus denitrificans lysates. The antibodies did not show reactivity with bovine heart cytochrome c oxidase either by ELISA or immunoblotting. It was also shown that the antibodies react with a single polypeptide present in Paracoccus denitrificans cell lysates, having an apparent molecular weight close to that of subunit III of bovine heart oxidase.
已获得针对一种合成十二肽的多克隆抗体，该十二肽与反硝化副球菌细胞色素c氧化酶亚基III的氨基酸序列120 - 131 DSPIKDGVWPPE（由其DNA序列推导得出）相同。当针对抗原进行测试时，这些抗体的效价高于1:10000。这些抗体已被用于提供免疫学证据，证明尽管亚基III未与细胞色素c氧化酶一起分离出来，但它存在于反硝化副球菌裂解物中。通过酶联免疫吸附测定（ELISA）或免疫印迹法，这些抗体均未显示出与牛心脏细胞色素c氧化酶的反应性。还表明，这些抗体与反硝化副球菌细胞裂解物中存在的一种单一多肽发生反应，该多肽的表观分子量与牛心脏氧化酶亚基III的表观分子量相近。
