کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1191683 | 963578 | 2006 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and identification of angiotensin I-converting enzyme inhibitory peptide from buckwheat (Fagopyrum esculentum Moench)
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated and identified from buckwheat (Fagopyrum esculentum Moench). Buckwheat protein extract was prepared by stirring in water (pH 9.0) for 30 min, followed by centrifugation at 15,000g for 20 min. The protein extract was then filtered using an YM-10 membrane. An ACE inhibitor was purified using consecutive chromatographic methods including: ion-exchange chromatography, gel filtration chromatography, and reverse-phase high performance liquid chromatography. The ACE inhibitor was identified to be a tripeptide, Gly-Pro-Pro, having IC50 value of 6.25 μg protein/ml, by protein sequencing system and electrospray-LC–mass spectrometry.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 96, Issue 1, May 2006, Pages 36–42
Journal: Food Chemistry - Volume 96, Issue 1, May 2006, Pages 36–42
نویسندگان
Min-Suk Ma, In Young Bae, Hyeon Gyu Lee, Cha-Bum Yang,