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Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sinapis alba L.
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  • Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sinapis alba L.
저자명
Yuk. Jin-Su,Lim. Young-Hee,Cho. Hong-Yon
간행물명
Journal of food science and nutrition
권/호정보
2000년|5권 2호|pp.75-80 (6 pages)
발행정보
한국식품영양과학회
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

To separate ACE inhibitors from edible plants, spices, and herbs, 285 extracts of 95 sources were screened for ACE inhibitory activity. The extract of Sinapis alba L. had the most potent ACE inhibitory activity. Mustard seeds were crushed homogeneously and extracted with hexane and water successively. Lyophilized water extract was fractionated with $H_2O$:butanol(1:1). The ACE inhibitor was purified from butanol fraction by methanol precipi-tation, gel filtration, HPLC, and FPLC with Superdex peptide HQ 10/30 column. The active fraction has been purified to homogeneity, which was proven by gel filtration using FPLC system. The yield was 0.02%. The com-pound has a molecular weight of about 640. The compound competitively inhibited ACE activity and the $IC_{50}$ value was 79$mu extrm{g}$/ml. The purified compound showed uterus contraction activity in isolated rat uterus.