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Abstract
Isolation and Characterization of Multiple Forms of Friabilin. Journal of Cereal Science 21:167-174
Morris,C.F., Greenblatt,G.A., Bettge,A.D. and Malkawi,H.I.
The control of endosperm texture on wheat grain is poorly understood at the molecular level. This study reports the isolation and partial characterization of multiple forms of friablilin a starch granule protein associated with endosperm softness. Starch granule proteins were isolated from water-washed wheat starch using sodium dodecyl sulfate (SDS), NaCl, propan-2-ol or NaCl plus propan-2-ol. SDS polyacrylamide gel electrophoresis under unreduced conditions revealed the presence of at least three components of what we all the Mr 15k complex, i.e. starch granule proteins of ca. Mr 15k, which have been considered previously to be single protein, friabilin. Based on selective extraction from starch, a fourth component may also be present. One of these four components may by as alpha-amylase inhibitor reported previously. N-terminal amino acid sequence data suggest that major components of the Mr 15k complex may by similar to Triton x-114-extractable proteins, termed puroindolines, isolated from wheat flour. Members of the Mr 15k complex shared similar dehydration-denaturation characteristics based on selective acetone precipitation. The results indicate that the operational use of friabilin as a discrete, single protein associated with endosperm texture, and possibly involved in texture control, must be re-evaluated. Nevertheless, friabilin remains a useful though enigmatic, biochemical marker for grain softness.
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