Cereal Chem 52:298 - 304.  |  VIEW ARTICLE
Albumin Pools with Different Extraction Behaviors in Wheat Seed.

M. Minetti, G. Morisi, V. Silano, and N. Accardi. Copyright 1975 by the American Association of Cereal Chemists, Inc. 

Several consecutive extractions with water failed to extract wheat albumins completely from whole wheat flour; a significant amount of these albumins (about one-third the amount extracted by water) could be extracted only by salt solutions. A 0.26M (NH4)2SO4 solution was the most suitable for extraction of this albumin fraction. Two albumin fractions were obtained by salting out the first water extract from flour with (NH4)2SO4 between 0.4 and 1.8M (albumin I) and between 1.8 and 4.0M (albumin II). Only one albumin fraction (albumin III) was obtained from the 0.26M (NH4)2SO4 extract of the flour residue remaining after five consecutive water extractions. Although different in their extraction behaviors, albumin I and albumin III fractions were both soluble in distilled water and were precipitated from the wheat extract in the same concentration range of (NH4)2SO4 (0.4 to 1.8M). When submitted to polyacrylamide-gel electrophoresis, these albumin fractions were both heterogeneous with slightly different electrophoretic patterns. Moreover, they exhibited identical staining properties with aniline blue-black as well as similar gel filtration and amino acid patterns. These data are consistent with the presence in wheat kernel of two closely related albumin pools, one of the two being bound by salt linkages to some water-insoluble components of the seed.