ACE Inhibitory Activity and Characteristics of Tri-Peptides Obtained from Bonito Protein
Author:
Affiliation:
1. Graduate School of Science and Technology, Kobe University
2. Department of Bioscience and Biotechnology, Okayama University
3. Department of Biosphere Sciences, Kobe College
Publisher
Society of Chemical Engineers, Japan
Subject
General Chemical Engineering,General Chemistry
Link
http://www.jstage.jst.go.jp/article/jcej/40/1/40_1_59/_pdf
Reference10 articles.
1. Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.
2. Purification and characterization of a novel antimicrobial peptide from maize (Zea mays L.) kernels.
3. Fujita, H., K. Yokoyama and M. Yoshikawa; “Classification and Antihypertensive Activity of Angiotensin I-Converting Enzyme Inhibitory Peptides Derived from Food Proteins,” J. Food Sci., 65, 4564–4569 (2000)
4. Hasan, F., M. Kitagawa, Y. Kumada, N. Hashimoto, M. Shiiba, S. Katoh and M. Terashima; “Production Kinetics of Angiotensin-I Converting Enzyme Inhibitory Peptides from Bonito Meat in Artificial Gastric Juice,” Process Biochem., 41, 505–511 (2006a)
5. Fragmentation of Angiotensin-I Converting Enzyme Inhibitory Peptides from Bonito Meat Under Intestinal Digestion Conditions and their Characterization
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