Biochemical and molecular characterization of an antifungal protein from Tenebrio molitor larvae

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We have purified an antifungal protein, named tenecin 3, from meal worms (larvae of Tenebrio molitor) by a combination of heat treatment, C-18 reverse-phase open column chromatography, and C-18 reverse-phase high performance liquid chromatography. A cDNA region containing coding information for tenecin 3 was identified by means of PCR-amplification with a degenerate primer inferred from its partial amino acid sequence. Analysis of cDNA indicated that tenecin 3 was composed of 78 amino acids and generated from a 96-amino acid precursor molecule. Tenecin 3 is rich in glycine (43.6% in molar percent) and has a repeated motif of Gly-X-X-Gly where X denotes glutamine, histidine, or leucine. This motif reiterates 11 times in tenecin 3. Comparative analysis of tenecin 3 and other antifungal proteins from different insects provides evidence for the existence of a family of antifungal proteins.
Publisher
Korean Soc Molecular & Cellular Biology
Issue Date
1995-01
Article Type
Article
Keywords

DERIVATIZATION; HEMOLYMPH; CLEAVAGE

Citation

MOLECULES AND CELLS, v.5, no.3, pp.287 - 292

ISSN
1016-8478
URI
http://hdl.handle.net/10203/71770
Appears in Collection
BS-Journal Papers(저널논문)
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