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应用
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
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
监管及禁止进口产品
从最新的版本中选择一种：
分析证书(COA)
Lot/Batch Number
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.
D W Cushman et al.
Biochemical pharmacology, 20(7), 1637-1648 (1971-07-01)
V Vermeirssen et al.
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
Go Eun Ha et al.
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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