Cereal Chem 47:447 - 463.  |  VIEW ARTICLE
Soluble Proteins of Wheat. III. Isolation and Characterization of Two Albumins, ALB 13A and ALB 13B, from Flour.

P. Feillet and C. C. Nimmo. Copyright 1970 by the American Association of Cereal Chemists, Inc. 

Two albumins were purified from extracts of common wheat flour through consecutive fractions by preparative free-flow electrophoresis, gel-permeation chromatography (Sephadex G-50), and DEAE- cellulose chromatography. The isolated proteins, designated ALB 13A and ALB 13B by the Feillet system, were homogeneous in polyacrylamide and starch-gel electrophoresis at pH 3.1 and 8.4. They had the same mobility, -2.5 x 10(-5) cm2 sec.-1 volt-1, in free electrophoresis in veronal buffer at pH 8.6. ALB 13A contained all the common amino acids, with alanine predominating, and no free sulfhydryl. ALB 13A had a relatively high valine content, no phenylalanine, histidine, or free sulfhydryl. Molecular-weight values for 13A were 24,800, 20,100, and 19,800 from sedimentation equilibrium, amino acid analysis, and gel- permeation chromatography, respectively. For 13B, corresponding values were 13,900, 12,900 and 11,200. E[1 percent/1 cm] was 13.35 (278 millimicrons) and 20.50 (274 millimicrons) for 13A and 13B. Fluorescence spectra were typical of tryptophan-containing proteins. Circular dichroism measurements suggested 25 to 30% alpha-helix for 13A, about 40% for 13B. ALB 13A and ALB 13B are apparently absent from durum wheats.