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Cereal Chem 52:719 - 725.  |  VIEW ARTICLE
Amino Acid Composition and Subunit Structure of Rye Gliadin Proteins Fractionated by Gel Filtration.

K. R. Preston and W. Woodbury. Copyright 1975 by the American Association of Cereal Chemists, Inc. 

Gliadins of rye (Secale cereale cv. Prolific) were separated by gel filtration on Sephadex G-100 into four distinct groups with apparent molecular weights (mol wt) of greater than 100,000 and 44,000, 27,000, and 10,000. These fractions contained 61, 29, 7, and 3% by weight of the total recovered protein, respectively. Each fraction had a distinct amino acid composition with the highest mol wt fraction having high glutamic acid and proline contents, whereas the two lowest mol wt fractions had amino acid compositions resembling albumins and globulins. Polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulfate before and after reduction was carried out on each fraction to determine subunit structure. The highest mol wt fraction gave five bands, all with apparent mol wt between 150,000 and 300,000, but after reduction of disulfide bonds only one band of mol wt 110,000 was present. The fractions of mol wt 44,000 and 27,000 from gel filtration each gave a single band with mol wt 42,000. The low-mol wt fraction had a single band of mol wt 10,000.

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