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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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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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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