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

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dc.contributor.authorChung, Jae Hoonko
dc.date.accessioned2013-02-28T00:35:34Z-
dc.date.available2013-02-28T00:35:34Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued1995-01-
dc.identifier.citationMOLECULES AND CELLS, v.5, no.3, pp.287 - 292-
dc.identifier.issn1016-8478-
dc.identifier.urihttp://hdl.handle.net/10203/71770-
dc.description.abstractWe 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.-
dc.publisherKorean Soc Molecular & Cellular Biology-
dc.subjectDERIVATIZATION-
dc.subjectHEMOLYMPH-
dc.subjectCLEAVAGE-
dc.titleBiochemical and molecular characterization of an antifungal protein from Tenebrio molitor larvae-
dc.typeArticle-
dc.identifier.wosidA1995RF21100016-
dc.type.rimsART-
dc.citation.volume5-
dc.citation.issue3-
dc.citation.beginningpage287-
dc.citation.endingpage292-
dc.citation.publicationnameMOLECULES AND CELLS-
dc.contributor.localauthorChung, Jae Hoon-
dc.type.journalArticleArticle-
dc.subject.keywordPlusDERIVATIZATION-
dc.subject.keywordPlusHEMOLYMPH-
dc.subject.keywordPlusCLEAVAGE-
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