Acein-1, a novel angiotensin-I-converting enzyme inhibitory peptide isolated from tryptic hydrolysate of human plasma
β Scribed by Kazuya Nakagomi; Akiyoshi Fujimura; Hidetoshi Ebisu; Tomomi Sakai; Yutaka Sadakane; Noriko Fujii; Takenori Tanimura
- Book ID
- 117109942
- Publisher
- Elsevier Science
- Year
- 1998
- Tongue
- English
- Weight
- 74 KB
- Volume
- 438
- Category
- Article
- ISSN
- 0014-5793
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Mung bean protein isolates were hydrolyzed for 2 h by Alcalase. The generated hydrolysate showed angiotensin I-converting enzyme (ACE) inhibitory activity with the IC(50) value of 0.64 mg protein/ml. Three kinds of novel ACE inhibitory peptides were isolated from the hydrolysate by Sephadex G-15 and
## Abstract Angiotensin Iβconverting enzyme (ACE) inhibitory peptide was isolated from wheat gliadin hydrolysate prepared with acid protease. Consecutive purification methods were used for peptide isolation including ionβexchange chromatography, sizeβexclusion chromatography, and reverseβphase high