Protein purification and nucleotide sequence of a lysozyme from the bacteria-induced larvae of the fall webworm, Hyphantria cunea

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Title
Protein purification and nucleotide sequence of a lysozyme from the bacteria-induced larvae of the fall webworm, Hyphantria cunea
Author(s)
Ho Yong Park; Soon Sik Park; Sang Woon Shin; Doo Sang Park; Mi Gwang Kim; Hyun Woo Oh; Chang Kyeong Joo
Bibliographic Citation
Archives of Insect Biochemistry and Physiology, vol. 35, no. 3, pp. 335-345
Publication Year
1997
Abstract
A protein with lytic activity against Micrococcus luteus was purified from the hemolymph of the fall webworm, Hyphantria cunea, larvae challenged with live E. coli. A bacteriolytic protein of about 14,000 daltons in mass was purified by cation exchange chromatography and reverse-phased HPLC. The optimum pH and optimum temperature range for activity were around pH 6.2 and 50°C, respectively, in a 100 mM phosphate buffer. The amino-terminal amino acid sequence of this protein was determined and the corresponding cDNA was isolated and analyzed. The deduced protein of 142 amino acid residues was composed of a putative leader sequence of 20 residues and the mature enzyme of 122 residues. The cloned lysozyme gene was strongly induced in response to bacterial injection, implying that the enzyme is a part of the immune response of H. cunea. Comparison with other known lysozyme sequences shows that our lysozyme belongs to the chicken lysozyme.
Keyword
Hyphantria cunealysozymeimmunityprotein sequencenucleotide sequencefall webworm
ISSN
0739-4462
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/(SICI)1520-6327(199705)35:3<335::AID-ARCH7>3.0.CO;2-S
Type
Article
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Jeonbuk Branch Institute > Biological Resource Center > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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