Benouareth D E, Dhainaut-Courtois N, Porchet-Hennere E, Curgy J J
CNRS UA 148, Université de Lille-Flandres-Artois, Villeneuve-d'Ascq, France.
Biol Cell. 1989;67(2):167-71.
The presence in the marine worm Nereis diversicolor of a low molecular mass protein with the capacity to bind cadmium has been previously demonstrated. Poly(A)(+)-mRNA were extracted from coelomocytes of Nereis diversicolor and were translated either in vitro, using a rabbit reticulocyte lysate, or in vivo into Xenopus laevis oocytes. Analysis of synthesized polypeptides by enzyme-linked immunosorbent assay (ELISA) and by Western blotting, using a specific monoclonal anti-MP II antibody, showed that this metalloprotein was translated both in in vitro and in vivo translation systems, with an apparent molecular mass of 11-13 kDa. Two other products, with 26.5 and 28 kDa molecular mass, cross-reacted with the monoclonal anti-MP II antibodies. The present work confirms that coelomocytes are sites of important synthesis of MP II-mRNA.
先前已证明,多毛纲海洋蠕虫杂色沙蚕中存在一种具有结合镉能力的低分子量蛋白质。从杂色沙蚕的体腔细胞中提取了聚腺苷酸(Poly(A)(+))mRNA,并在体外使用兔网织红细胞裂解物进行翻译,或在体内注入非洲爪蟾卵母细胞中进行翻译。通过酶联免疫吸附测定(ELISA)和蛋白质免疫印迹法,使用特异性单克隆抗MP II抗体对合成多肽进行分析,结果表明这种金属蛋白在体外和体内翻译系统中均有翻译,其表观分子量为11 - 13 kDa。另外两种分子量分别为26.5 kDa和28 kDa的产物与单克隆抗MP II抗体发生交叉反应。目前的研究工作证实,体腔细胞是MP II - mRNA重要的合成场所。