Isolation and characterization of Korean pine (Pinus koraiensis) convicilin

被引：9

作者：

Jin, Tengchuan ^{[1
]}

Wang, Yang ^{[1
]}

Chen, Yu-Wei ^{[1
]}

Albillos, Silvia M. ^{[2
]}

Kothary, Mahendra H. ^{[3
]}

Fu, Tong-Jen ^{[4
]}

Tankersley, Boyce ^{[5
]}

McHugh, Tara H. ^{[6
]}

Zhang, Yu-Zhu ^{[1
,6
]}

机构：

[1] Illinois Inst Technol, Dept Biol & Chem Sci, Chicago, IL 60616 USA

[2] Illinois Inst Technol, Inst Food Safety & Hlth, Bedford Pk, IL 60501 USA

[3] US FDA, Ctr Food Safety & Appl Nutr, Laurel, MD 20708 USA

[4] US FDA, Inst Food Safety & Hlth, Bedford Pk, IL 60501 USA

[5] Chicago Bot Garden, Chicago, IL 60022 USA

[6] USDA ARS, Hlth Proc Foods Res Unit, Western Reg Res Ctr, Albany, CA 94710 USA

来源：

PLANT PHYSIOLOGY AND BIOCHEMISTRY | 2014年 / 80卷

关键词：

Storage protein; Chemical denaturation; Stability; Potential allergen; Protein folding; PISUM-SATIVUM-L; SEED STORAGE PROTEIN; MAJOR ALLERGENS; PEA VICILIN; NUTS; PURIFICATION; ANAPHYLAXIS; SUBUNITS;

D O I：

10.1016/j.plaphy.2014.03.019

中图分类号：

Q94 [植物学];

学科分类号：

071001 [植物学];

摘要：

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 degrees C compared with 84.13 degrees 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 C-m of 4.41 +/- 0.15 M. Published by Elsevier Masson SAS.

引用

页码：97 / 104

页数：8

共 25 条

[1]

BASIC LOCAL ALIGNMENT SEARCH TOOL [J].

ALTSCHUL, SF ;

GISH, W ;

MILLER, W ;

MYERS, EW ;

LIPMAN, DJ .

JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410

[2]

Ano M A, 2002, Allergol Immunopathol (Madr), V30, P104

[3]

UNFOLDING FREE-ENERGY CHANGES DETERMINED BY THE LINEAR EXTRAPOLATION METHOD .2. INCORPORATION OF DELTA-G-DEGREES-N-U VALUES IN A THERMODYNAMIC CYCLE [J].

BOLEN, DW ;

SANTORO, MM .

BIOCHEMISTRY, 1988, 27 (21) :8069-8074

[4]

Pine nut allergy: Clinical features and major allergens characterization [J].

Cabanillas, Beatriz ;

Cheng, Hsiaopo ;

Grimm, Casey C. ;

Hurlburt, Barry K. ;

Rodriguez, Julia ;

Crespo, Jesus F. ;

Maleki, Soheila J. .

MOLECULAR NUTRITION & FOOD RESEARCH, 2012, 56 (12) :1884-1893

[5]

CONVICILIN MESSENGER-RNA FROM PEA (PISUM-SATIVUM-L) HAS SEQUENCE HOMOLOGY WITH OTHER LEGUME 7S STORAGE PROTEIN MESSENGER-RNA SPECIES [J].

CASEY, R ;

DOMONEY, C ;

STANLEY, J .

BIOCHEMICAL JOURNAL, 1984, 224 (02) :661-666

[6]

THE PURIFICATION AND CHARACTERIZATION OF A 3RD STORAGE PROTEIN (CONVICILIN) FROM THE SEEDS OF PEA (PISUM-SATIVUM-L) [J].

CROY, RRD ;

GATEHOUSE, JA ;

TYLER, M ;

BOULTER, D .

BIOCHEMICAL JOURNAL, 1980, 191 (02) :509-516

[7]

A comparative study of convicilin storage protein gene sequences in species of the tribe Vicieae [J].

de Miera, L. E. Saenz ;

Ramos, J. ;

de la Vega, M. Perez .

GENOME, 2008, 51 (07) :511-523

[8]

Carboxypeptidase I from triticale grains and the hydrolysis of salt-soluble fractions of storage proteins [J].

Drzymala, Adam ;

Prabucka, Beata ;

Bielawski, Wiesiaw .

PLANT PHYSIOLOGY AND BIOCHEMISTRY, 2012, 58 :195-204

[9]

FINE AJ, 1987, ANN ALLERGY, V59, P183

[10]

A 17-kDa allergen detected in pine nuts [J].

García-Menaya, JM ;

Gonzalo-Garijo, MA ;

Moneo, I ;

Fernández, B ;

García-González, F ;

Moreno, F .

ALLERGY, 2000, 55 (03) :291-293

← 1 2 3 →