한빛사 논문
Abstract
Bo-Hye Nama, 1,*, Jung-Kil Seob, 1, Min Jeong Leec, Young-Ok Kima, Dong-Gyun Kima, Cheul Min Ana, Nam Gyu Parkc,*
a Biotechnology Research Division, National Fisheries Research and Development Institute, Busan 619-902, Republic of Korea
b Department of Food Science and Biotechnology, Kunsan National University, Kunsan 573-701, Republic of Korea
c Department of Biotechnology, Pukyoung National University, Busan 608-737, Republic of Korea
*Corresponding author : Bo-Hye Nam, Nam Gyu Park
1 Both authors contributed equally to this work.
Abstract
An antimicrobial peptide, ∼5 kDa in size, was isolated and purified in its active form from the mantle of the Pacific oyster Crassostrea gigas by C18 reversed-phase high-performance liquid chromatography. Matrix-assisted laser desorption ionisation time-of-flight analysis revealed 4656.4 Da of the purified and unreduced peptide. A comparison of the N-terminal amino acid sequence of oyster antimicrobial peptide with deduced amino acid sequences in our local expressed sequence tag (EST) database of C. gigas (unpublished data) revealed that the oyster antimicrobial peptide sequence entirely matched the deduced amino acid sequence of an EST clone (HM-8_A04), which was highly homologous with the β-thymosin of other species. The cDNA possessed a 126-bp open reading frame that encoded a protein of 41 amino acids. To confirm the antimicrobial activity of C. gigas β-thymosin, we overexpressed a recombinant β-thymosin (rcgTβ) using a pET22 expression plasmid in an Escherichia coli system. The antimicrobial activity of rcgTβ was evaluated and demonstrated using a bacterial growth inhibition test in both liquid and solid cultures.
Keywords : Pacific oyster (Crassostrea gigas); Thymosin; Antimicrobial activity; Recombinant protein
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