earticle

영어

We have investigated for amino acid composition and molecular weight of the sunflower main protein which was purfied by Sephadex column. The results were obtained as fellow. 1. The salt-soluble sunflower proteins were highly dispersible in 0.02M sodium phosphate buffer, containing 10% sodium chloride. 2. The sunflower proteins were characterized by comparatively high levels of essential amino acids. 3. Seven bands of component of sunflower proteins were found in disc electrophoretic gel column. 4. The sunflower main protein was purified by Sephadex G-150 and A-25 column chromatography 5. The molecular weight was estimated 86,000 for the sunflower main protein.

한국어

한국에서 재배된 해바라기(Helianthus annus)씨 단백질의 화학적 성질을 규명하고자 이의 염용해성 단백질을 추출한 다음 정제하여 주단백질을 분리하여 본 결과 1. 염용해성 단백질의 추출용매는 10% 염화나트륨을 함유한 0.02M sodium phosphate buffer가 가장 좋았다. 2. 해바라기씨 단백질의 필수아미노산 조성은 비교적 양질인 것으로 나타났다. 3. 염용해성단백질의 disc전기이동에서 7개의 band를 나타내었다. 4. 염용해성단백질의 주단백질은 Sephadex G-150과 A-25 column으로 정제하여 얻을 수 있었다. 4. 주단백질의 분자량은 약 86,000이였다.