Studies on the Isolation of Albumin and Globulin from Wheat Germ Protein

Wheat germ protein was extracted and isolated by a Modified Osborne fractionation method and some properties were investigated. The results are summarized as follows; 1. Approximate compositions of wheat germ were moisture 10.5%, crude protein 22.8%, crude fat 2.4%, crude ash 3.2%, crude fiber 1.5%, respectively. 2. Nitrogen solubilities on various solvents were the lowest as 45.58% by Osborne method and the highest as 79.49% after sequencial extraction of the , 0.5M-NaCl, 70%-ethanol, 0.1N-NaOH. 3. Isolated proteins yielded albumin, globulin, globulin, gliadin and glutelin in the proportion of 20.22: 17.49: 42.58: 19.71, respectively. 4. Spectrophometric chromatograms of isolated protein by Regel-filtration were two peaks in albumin (I ; 8.2%, II ; 91.8%), one peak in globulin (92.8%), respectively. 5. Disc-PAGE patterns were showed about 14 bands in 0.5M-Cl soluble protein, 3bands in crude albumin, 1band in main albumin, 2bands in crude globulin, one band in main globulin under pH 8.3 buffer system (Ornstein and Davis method).