밀배아단백질은 Modified Osborne방법에 의해 추출 분리하여 그의 몇가지 특성을 조사한 결과는 다음과 같다. 1. 밀배아의 일반성분 분석중 조단백질 함량은 22.8%로 나타났다. 2. 여러 용매에 의한 단백질 용해도는 종래의 Osborne방법이 45.58%로 가장 낮았고 $H_2O$, 0.5M-NaCl, 70% ethanol, 0.1N-NaOH의 순으로 추출한 경우가 79.49%로 가장 높았다. 3. 분리단백질의 분포는 albumin이 20.22% globulin이 17.49%, gliadin이 42.58%, glutelin이 19.71% 이었다. 4. Regel-filtration에 의해 분리된 단백질의 Chromatogram은 albumin이 2개의 peak(I ; 8.2% II ; 91.8%)로 나타났으며 globulin은 1개의 peak로 나타났다. 5. Ornstein과 Davis의 방법(pH 8.3)으로 전기 영동한 결과 0.5M-NaCl soluble protein은 약 14개의 band로, albumin은 crude가 3개 main albumin이 1개의 균일한 band로 나타났으며 globulin은 crude가 2개의 band, main globulin은 1개의 균일한 band로 나타났다.
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 $H_2O$, 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).
