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

Archives of Insect Biochemistry and Physiology
H Y ParkC K Joo

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 degrees 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.

References

Jan 1, 1987·Annual Review of Microbiology·H G Boman, D Hultmark
Jul 15, 1973·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·R F Powning, W J Davidson
Sep 1, 1984·Molecular and Cellular Biochemistry·P Jollès, J Jollès
Mar 1, 1994·Insect Biochemistry and Molecular Biology·A B Mulnix, P E Dunn

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