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OALib Journal期刊
ISSN: 2333-9721
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Isolation and Purification of the Fused Protein Encoded by Synthetic Antigen Gene of Plasmodium Falciparum and Its Expression in Escherichia coli
恶性疟合成多肽抗原基因在大肠杆菌中表达产物的分离纯化

Keywords: Plasmodium falciparum,antigen gene expression,protein isolation and purification,polyacrylamide gel electrophoresis
疟疾
,疟原虫,合成多肽,抗原,表达产物,提纯

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Abstract:

The fusion protein from synthesized plasmodium falciparum hybrid antigen gene expressed in E. colt was purified. The recombinants (pWR/A ?7,pWR/B ?164, pWR/AB ?20)grew in Luria broth medium with lactose. The bacteria were harvested by centrifugation and the pelleted cells were, suspended in lysis buffer containing NP-40 and lysozyme and were treated by sonication and centrifugation. The fusion protein was isolated with SDS-PAGE and recovered by electrophoresis. One to four mg pure fusion protein can be obtained from 80-100 ml bacterial culture media. (Rabbits were immunized by the purified fusion protein and serologic assay has demonstrated with immuno-geneicity).

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