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Design of signal peptide bombyxin and its effect on secretory expression efficiency and levels of Helicobacter pylori urease subunit B in silkworm cells and larvae BABT
Zhang,Xiao-lin; Jiang,An-min; Ma,Zhong-you; Xiong,You-yi; Dou,Jin-feng; Zhou,Guo-liang; Qin,Mei-song; Wang,Jian-fei.
This study employed a Bac-to-Bac/Bombyx mori bioreactor to mass-produce immunogenic urease subunit B (UreB) from Helicobacter pylori.The signal peptide bombyxin from B. mori was used to promote secretory expression to improve expression levels and was designed and integrated into the UreB gene to generate the Bacmid/BmNPV/(signal peptide)-UreB baculovirus expression system. To determine whether the bombyxin signal peptide resulted in secretory expression of recombinant UreB (rUreB) and to determine the secretory efficiency, we tested the secretory expression level of rUreB in Bm5 cells using ELISA. To further investigate whether secretory expression affected cell viability, cells were evaluated using 0.4% trypan blue staining, and Bacmid/BmNPV/UreB without...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Baculovirus expression system; Bombyx mori; Signal peptide; Helicobacter pylori urease subunit B; Secretory expression.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000300319
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Molecular characterization and transcriptome profiling of expansin genes isolated from Calotropis procera fibers Electron. J. Biotechnol.
Cheema,Hafiza Masooma Naseer; Bashir,Aftab; Khatoon,Asia; Iqbal,Nadia; Zafar,Yusuf; Malik,Kauser A.
The Calotropis procera seed fibers provide an excellent model system to study the genes involved in fiber elongation, fineness and strength. Expansins constitute one of the important gene families involved in plant cell expansion and other cell wall modification processes. Four homologs of Expansin A gene i.e. CpEXPA1, CpEXPA2, CpEXPA3 and CpEXPA4 were isolated from the cDNA library obtained from fast growing Calotropis procera fibers. These homologs represented typical Expansin A family. Each of them had two conserved domains including GH45 like domain and the putative polysaccharide binding domain. The deduced amino acid sequences of the homologs indicated three conserved motifs: i) eight cysteine residues at N-terminus, ii) four tryptophan residues at...
Tipo: Journal article Palavras-chave: Calotropis procera; CDNA library; Cotton fibers; EXPANSIN A; Signal peptide; Transcriptome profiling.
Ano: 2010 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582010000600010
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