title: Isolation and characterization of Korean pine (Pinus koraiensis) convicilin.
abstract: A vicilin-like globulin seed storage protein, termed convicilin, was isolated for the first time from Korean pine (Pinus koraiensis). SDS-PAGE analysis revealed that Korean pine convicilin was post-translationally processed. The N-terminal peptide sequences of its components were determined. These peptides could be mapped to a protein translated from an embryo abundant transcript isolated in this study. Similar to vicilin, native convicilin appeared to be homotrimeric. Differential scanning calorimetry (DSC) analyses revealed that this protein is less resistant to thermal treatment than Korean pine vicilin. Its transition temperature was 75.57 °C compared with 84.13 °C for vicilin. The urea induced folding-unfolding equilibrium of pine convicilin monitored by intrinsic fluorescence could be interpreted in terms of a two-state model, with a Cm of 4.41 ± 0.15 M.
authors.affiliation: Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA. Electronic address: jint@niaid.nih.gov.
authors.forename: Tengchuan
authors.initials: T
authors.lastname: Jin
authors.affiliation: Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA.
authors.forename: Yang
authors.initials: Y
authors.lastname: Wang
authors.affiliation: Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA.
authors.forename: Yu-Wei
authors.initials: YW
authors.lastname: Chen
authors.affiliation: Institute for Food Safety and Health, Illinois Institute of Technology, 6502 South Archer Road, Bedford Park, IL 60501, USA.
authors.forename: Silvia M
authors.initials: SM
authors.lastname: Albillos
authors.affiliation: Center for Food Safety and Applied Nutrition, U.S. Food & Drug Administration, Laurel, MD 20708, USA.
authors.forename: Mahendra H
authors.initials: MH
authors.lastname: Kothary
authors.affiliation: Institute for Food Safety and Health, U.S. Food & Drug Administration, 6502 South Archer Road, Bedford Park, IL 60501, USA.
authors.forename: Tong-Jen
authors.initials: TJ
authors.lastname: Fu
authors.affiliation: Chicago Botanic Garden, Glencoe, IL 60022, USA.
authors.forename: Boyce
authors.initials: B
authors.lastname: Tankersley
authors.affiliation: Healthy Processed Foods Research Unit, USDA-ARS, Western Regional Research Center, 800 Buchanan Street, Albany, CA 94710, USA.
authors.forename: Tara H
authors.initials: TH
authors.lastname: McHugh
authors.affiliation: Healthy Processed Foods Research Unit, USDA-ARS, Western Regional Research Center, 800 Buchanan Street, Albany, CA 94710, USA; Department of Biological and Chemical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA. Electronic address: yuzhu.zhang@ars.usda.gov.
authors.forename: Yu-Zhu
authors.initials: YZ
authors.lastname: Zhang
mesh_terms: D004591:Electrophoresis, Polyacrylamide Gel; D028223:Pinus / Q000378:metabolism*; D017510:Protein Folding; D055314:Seed Storage Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D013696:Temperature
chemical_list: D055314:Seed Storage Proteins; C015575:vicilin protein, plant
keywords: Chemical denaturation; Potential allergen; Protein folding; Stability; Storage protein