Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801112 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2005 | 7 Pages |
Abstract
We have purified a novel antibacterial peptide from the hemolymph of the coleopteran insect Acalolepta luxuriosa, of the family Cerambyocidae, and named it luxuriosin. This peptide showed growth-inhibitory activity against Micrococcus luteus and germination- and/or growth-inhibitory activity against the conidia from rice blast fungus, Magnaporthe grisea. The amino acid sequence determined by cDNA cloning identified luxuriosin as a peptide of 88 amino acids with a theoretical molecular weight of 10,368.34, containing a Kunitz domain.
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Authors
Kenjiro Ueda, Ayaka Saito, Morikazu Imamura, Nami Miura, Shogo Atsumi, Hiroko Tabunoki, Ayako Watanabe, Madoka Kitami, Ryoichi Sato,