Small angle X-ray scattering of wheat seed-storage proteins:: α-, γ- and ω-gliadins and the high molecular weight (HMW) subunits of glutenin

被引:63
作者
Thomson, NH
Miles, MJ
Popineau, Y
Harries, J
Shewry, P
Tatham, AS
机构
[1] Univ Bristol, Long Ashton Res Stn, Dept Agr Sci, Bristol BS18 9AF, Avon, England
[2] Univ Bristol, HH Wills Phys Lab, Bristol BS8 1TL, Avon, England
[3] INRA, Lab Biochem & Technol Prot, F-44026 Nantes, France
[4] Daresbury Lab, EPSRC Synchrotron Radiat Source, Warrington WA4 4AD, Cheshire, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1999年 / 1430卷 / 02期
基金
英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;
关键词
gliadin; glutenin; small angle X-ray scattering;
D O I
10.1016/S0167-4838(99)00019-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Small angle X-ray scattering in solution was performed on seed-storage proteins from wheat. Three different groups of gliadins (alpha-, gamma- and omega-) and a high molecular weight (HMW) subunit of glutenin (1Bx20) were studied to determine molecular size parameters, All the gliadins could be modelled as prolate ellipsoids with extended conformations. The HMW subunit existed as a highly extended rod-like particle in solution with a length of about 69 nm and a diameter of about 6.4 nm, Specific aggregation effects were observed which may reflect mechanisms of self-assembly that contribute to the unique viscoelastic properties of wheat dough. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:359 / 366
页数:8
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