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Vrat Kamboj,Dev; Nema,Vijay; Kumar Pandey,Arun; Kumar Goel,Ajay; Singh,Lokendra. |
Staphylococcal food poisoning (SFP) is caused by the members of superantigen family called staphylococcal enterotoxins (SEs). About 20 different types of SEs are produced by Staphylococcus aureus out of which type A (SEA), B (SEB), C (SEC) and D (SED) are commonly implicated in SFP. Among these, SEB is the most potent toxin and has also gained the status of biological warfare (BW) agent. Therefore, detection of SEB is of utmost importance. Any immunological detection system for SEB requires specific and sensitive antibodies which inturn depends on the purity of the SEB. In the present investigation, seb gene of S. aureus was cloned and expressed in E. coli along with biotin as fusion partner to facilitate the purification process. The yield of purified... |
Tipo: Journal article |
Palavras-chave: Affinity purification; Biotin fusion; ELISA; Gene cloning; SEB; Western blot. |
Ano: 2006 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000500010 |
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Cong,Lina; Liang,Wenjing; Wu,Yao; Li,Cheng; Chang,Yihai; Dong,Liang; Song,Wanlin; Ma,Jun. |
Background The sea cucumber lysozyme belongs to the family of invertebrate lysozymes and is thought to be a key defense factor in protecting aquaculture animals against bacterial infection. Recently, evidence was found that the sea cucumber lysozyme exerts broad spectrum antimicrobial action in vitro against Gram-negative and Gram-positive bacteria, and it also has more potent antimicrobial activity independent of its enzymatic activity. To explore the antimicrobial role of this non-enzymatic lysozyme and model its structure to novel antimicrobial peptides, the peptide from the C-terminal amino acid residues 70-146 of the sea cucumber lysozyme in Stichopus japonicus (SjLys-C) was heterologously expressed in Escherichia coli Rosetta(DE3)pLysS. Results The... |
Tipo: Journal article |
Palavras-chave: Affinity purification; Lysozyme peptide; Molecular modeling; Recombinant protein. |
Ano: 2014 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000600005 |
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