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

밀 배아 단백질중 Albumin과 Globulin의 분리에 관한 연구

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).

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.