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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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