The insertion of bioactive peptides at the C-terminal end of an 11S globulin changes the structural stability and improves the antihypertensive activity
Open Access
- 1 January 2019
- journal article
- research article
- Published by Elsevier in Electronic Journal of Biotechnology
- Vol. 37, 18-24
Abstract
No abstract availableKeywords
Funding Information
- Secretaria de Investigación y Posgrado-IPN (20144006, 20171468)
- Secretaría de Ciencia, Humanidades, Tecnología e Innovación (103399, 256478)
This publication has 41 references indexed in Scilit:
- Manufacturing of peptides exhibiting biological activityAmino Acids, 2012
- Modification of the amaranth 11S globulin storage protein to produce an inhibitory peptide of the angiotensin I converting enzyme, and its expression in Escherichia coliJournal of Biotechnology, 2010
- Modeling of the Relationship between Dipeptide Structure and Dipeptide Stability, Permeability, and ACE Inhibitory ActivityJournal of Food Science, 2009
- The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular diseaseThe Journal of Nutritional Biochemistry, 2008
- Expression and characterization of the acidic subunit from 11S Amaranth seed proteinBiotechnology Journal, 2008
- Protein production by auto-induction in high-density shaking culturesProtein Expression and Purification, 2005
- Structure−Physicochemical Function Relationships of Soybean Glycinin at Subunit Levels Assessed by Using Mutant LinesJournal of Agricultural and Food Chemistry, 2004
- Crystal Structure of Soybean Proglycinin A1aB1b HomotrimerJournal of Molecular Biology, 2001
- Structural analysis of globulins isolated from genetically different Amaranthus hybrid linesFood Chemistry, 1998
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970