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Structure and heterogeneity of gliadin: a hydrodynamic evaluation |
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| Authors: | Shirley Ang Jana Kogulanathan Gordon A Morris M Samil Kök Peter R Shewry Arthur S Tatham Gary G Adams Arthur J Rowe Stephen E Harding |
| Institution: | 1. NCMH Laboratory, Division of Food Science, School of Biosciences, National Centre for Macromolecular Hydrodynamics (NCMH), University of Nottingham, Sutton Bonington, LE12 5RD, UK 2. Department of Food Engineering, Abant Izzet Baysal University (A?Bü), 14280, Bolu, Turkey 3. Centre for Crop Genetic Improvement, Rothamsted Research, Harpenden, Hertfordshire, AL5 2JQ, UK 4. Cardiff School of Health Sciences, University of Wales Institute Cardiff, Cardiff, CF5 2YB, UK 5. Insulin and Diabetes Experimental Research (IDER) Group, Faculty of Medicine and Health Science, University of Nottingham, Clifton Boulevard, Nottingham, NG7 2RD, UK |
| Abstract: | A study of the heterogeneity and conformation in solution in 70% (v/v) aq. ethanol] of gliadin proteins from wheat was undertaken based upon sedimentation velocity in the analytical ultracentrifuge, analysis of the distribution coefficients and ellipsoidal axial ratios assuming quasi-rigid particles, allowing for a range of plausible time-averaged hydration values. All classical fractions (α, γ, ωslow, ωfast) show three clearly resolved components. Based on the weight-average sedimentation coefficient for each fraction and a weight-average molecular weight from sedimentation equilibrium and/or cDNA sequence analysis, all the proteins are extended molecules with axial ratios ranging from ~10 to 30 with α appearing the most extended and γ the least. |
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