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Producing recombinant commercial proteins ArchiMer
Cadoret, Jean-paul; Bardor, M; Lerouge, P; Cabigliera, M; Henriquez, Vitalia; Carlier, Aude.
Extraction of natural substances and chemical synthesis are the main sources of pharmaceutical molecules. When possible, one may transfer the gene of the molecule in living cells creating individual factories producing on demand and in a safe way the requested molecule. Today, bacteria, yeast, mammalian cells and plants constitute the main plate-forms for various commercial products. Microalgae present numerous advantages and could offer a powerful tool for the production of commercial molecules in a near future.
Tipo: Text Palavras-chave: Genetics; Recombinant; Algae; Pharmaceuticals; Gene transfer; Biotechnology; Génétique; Recombinant; Algues; Pharmaceutique; Transfert de gène; Biotechnologie.
Ano: 2008 URL: http://archimer.ifremer.fr/doc/2008/publication-4045.pdf
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Heterologous expression, protein folding and antibody recognition of a neurotoxin from the Mexican coral snake Micrurus laticorallis J. Venom. Anim. Toxins incl. Trop. Dis.
Clement,Herlinda; Flores,Vianey; la Rosa,Guillermo De; Zamudio,Fernando; Alagon,Alejandro; Corzo,Gerardo.
Abstract Background The cysteine-rich neurotoxins from elapid venoms are primarily responsible for human and animal envenomation; however, their low concentration in the venom may hamper the production of efficient elapid antivenoms. Therefore, the aim of the present study was to produce fully active elapid neurotoxic immunogens for elapid antivenom production. Method Cysteine-rich neurotoxins showed recombinant expression in two strains of E. coli, and were purified using affinity chromatography and reverse-phase HPLC (rpHPLC). Results The cDNA of the four disulfide-bridged peptide neurotoxin Mlat1 was cloned into a modified expression vector, pQE30, which was transfected into two different E. coli strains. The recombinant toxin (HisrMlat1) was...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Micrurus laticorallis; Protein folding; Recombinant; Elapid; Toxin; Protein recognition.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100318
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Isolation and Analysis of Recombinant EPSP synthases from Microbial Pathogens for Drug Design Purpose Thai Agricultural
Vaithanomsat, P.; Brown, K..
Palavras-chave: Isolation; Analysis; Recombinant.
Ano: 1461 URL: http://anchan.lib.ku.ac.th/agnet/handle/001/5025
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Cloning and expression of Aujeszky's disease virus glycoprotein E (gE) in a baculovirus system BJM
Dambros,Régia Maria Feltrin; Ribeiro,Bergman Moraes; Aguiar,Raimundo Wagner de S.; Schaefer,Rejane; Esteves,Paulo Augusto; Perecmanis,Simone; Simon,Neide Lisiane; Silva,Nayara Cavalcante; Coldebella,Michele; Ciacci-Zanella,Janice Reis.
Aujeszky' s disease (AD) is an infectious disease causing important economic losses to the swine industry worldwide. The disease is caused by an alpha-herpesvirus, Aujeszky' s disease virus (ADV), an enveloped virus with a double stranded linear DNA genome. The ADV genome encodes 11 glycoproteins, which are major targets for the immune system of the host in response to the infection. The glycoprotein E (gE) is a non-essential protein and deletion of the gE gene has been used for the production of marker vaccines. Aiming to develop molecular reagents for the production of a gE specific ELISA test, the gE gene was amplified by PCR, cloned and expressed into a baculovirus expression system. The recombinant DNA vector pFastBac-gE-ADV was used for site-specific...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Aujeszky; Glycoprotein E; Baculovírus; Recombinant.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822007000300021
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