Recommended Products
Application
Lung acetone powder from rabbit has been used in the determination of angiotensin converting enzyme (ACE) inhibitory activity:
- from milk fermentate by Bifidobacterium longum
- in Caco-2 brush border expressing (Bbe) cell monolayer
- from ginger extracts
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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Physiological activities of ginger extracts originated from different habitat
Food Science and Biotechnology, 15(1), 143-147 (2006)
Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung.
Biochemical pharmacology, 20(7), 1637-1648 (1971-07-01)
Journal of peptide science : an official publication of the European Peptide Society, 8(3), 95-100 (2002-04-05)
ACE inhibitory peptides are biologically active peptides that play a role in blood pressure regulation. When derived from food proteins during food processing or gastrointestinal digestion, these peptides could function as efficient agents in treating and preventing hypertension. However, in
Korean journal for food science of animal resources, 35(6), 738-747 (2016-02-16)
Angiotensin-converting enzyme (ACE) inhibitory activity was evaluated for the low-molecular-weight fraction (<3 kDa) obtained from milk fermentation by Bifidobacterium longum KACC91563. The ACE inhibitory activity in this fraction was 62.3%. The peptides generated from the <3 kDa fraction were identified
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