Biochemical and Molecular Characterization of an Antifungal Protein from Tenebrio molitor Larvae
- Authors
- Jung, Young Hwan; Park, Byung Young; Lee, Dong-Ki; Hahn, Yoonsoo; Chung, Jae Hoon; Han, Dong Min; Moon, Hyun Joo; Lee, Bok Luel; Lee, Younghoon
- Issue Date
- Jun-1995
- Publisher
- 한국분자세포생물학회
- Citation
- Molecules and Cells, v.5, no.3, pp 287 - 292
- Pages
- 6
- Journal Title
- Molecules and Cells
- Volume
- 5
- Number
- 3
- Start Page
- 287
- End Page
- 292
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/59662
- ISSN
- 1016-8478
0219-1032
- Abstract
- We have purified an antifungal protein, named tenecin 3, from meal worms (larvae of Tenebrio molitor) by a combination of heat treatment, C18 reverse-phase open column chromatography, and C18 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 famiJy of antifungal proteins.
- Files in This Item
-
Go to Link
- Appears in
Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.