Devaney E
Department of Parasitology, Liverpool School of Tropical Medicine, U.K.
Mol Biochem Parasitol. 1988 Jan 1;27(1):83-92. doi: 10.1016/0166-6851(88)90027-8.
The major surface antigen (30 kDa) of Brugia pahangi has been characterised by a number of biochemical and immunochemical means. The 30 kDa polypeptide is a glycoprotein which can be extracted from the worm surface by homogenization in the absence of detergents. The 30 kDa polypeptide can be metabolically labelled with [35S]methionine in adult male and female parasites. In addition small amounts of the 35S-labelled 30 kDa antigen can be detected in the medium of worms cultured in vitro. 125I labelling of the excretory-secretory (ES) products of adult male and female parasites followed by immunoprecipitation and peptide mapping has confirmed the relationship between the surface located 30 kDa polypeptide and that released in vitro.
彭亨布鲁线虫的主要表面抗原(30 kDa)已通过多种生化和免疫化学方法进行了表征。30 kDa多肽是一种糖蛋白,可在无去污剂的情况下通过匀浆从虫体表面提取。30 kDa多肽可在成年雌雄寄生虫中用[35S]甲硫氨酸进行代谢标记。此外,在体外培养的虫体培养基中可检测到少量35S标记的30 kDa抗原。用125I标记成年雌雄寄生虫的排泄分泌(ES)产物,然后进行免疫沉淀和肽图谱分析,证实了位于表面的30 kDa多肽与体外释放的多肽之间的关系。