Affinity Purification and Molecular Characterization of Angiotensin-Converting Enzyme (ACE)-Inhibitory Peptides from Takifugu flavidus

Affinity Purification and Molecular Characterization of Angiotensin-Converting Enzyme (ACE)-Inhibitory Peptides from Takifugu flavidus

An affinity chromatography filler of CNBr-activated Sepharose 4B-immobilized ACE was used to purify ACE-inhibitory peptides from Takifugu flavidus protein hydrolysate (

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Veröffentlicht in:Marine drugs 2023-09, Vol.21 (10), p.522
Hauptverfasser: Su, Yongchang, Chen, Shicheng, Liu, Shuji, Wang, Yin, Chen, Xiaoting, Xu, Min, Cai, Shuilin, Pan, Nan, Qiao, Kun, Chen, Bei, Yang, Suping, Liu, Zhiyu
Format: Artikel
Sprache:eng
Schlagworte:
ACE-inhibitory activity
Affinity
Affinity chromatography
affinity purification
Amino acids
Angiotensin
antihypertensive effect
Antihypertensives
Binding sites
Blood pressure
Chromatography
Electrostatic properties
Enzymes
Hydrogen bonds
Hydrolysates
Hydrophobicity
Hypertension
Molecular docking
Molecular interactions
Peptides
Peptidyl-dipeptidase A
Protein purification
Proteins
R&D
Research & development
Simulation
Sodium chloride
Surface plasmon resonance
Takifugu flavidus
Water purification
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Zusammenfassung:An affinity chromatography filler of CNBr-activated Sepharose 4B-immobilized ACE was used to purify ACE-inhibitory peptides from Takifugu flavidus protein hydrolysate (
ISSN:1660-3397
1660-3397
DOI:10.3390/md21100522