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A6778

Sigma-Aldrich

Angiotensin Converting Enzyme from rabbit lung

≥2.0 units/mg protein (modified Warburg-Christian)

Synonym(s):

ACE, Peptidyl-dipeptidase A, Peptidyldipeptide Hydrolase

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About This Item

CAS Number:
Enzyme Commission number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
42010109
NACRES:
NA.32

form

lyophilized powder

Quality Level

specific activity

≥2.0 units/mg protein (modified Warburg-Christian)

shipped in

dry ice

storage temp.

−20°C

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General description

The angiotensin-converting enzyme (ACE) is a dipeptidyl-carboxypeptidase which exists in somatic and testicular isoforms with zinc binding motif HEXXH in their active site. ACE regulates blood pressure through renin-angiotensin system. ACE elevates blood pressure by converting angiotensin I to a key vasoconstrictor angiotensin II and inhibiting a potent vasodilator bradykinin. Inhibition of ACE is a targeted therapeutic strategy for high blood pressure. Several ACE synthetic inhibitory peptides available for clinical use include captopril, enalapril and lisinopril. Currently, developing inhibitory peptides from natural food sources, or phenolic compounds from plant sources to inhibit ACE is underway. ACE plays a critical role in fertilization by releasing the proteins anchored to glycosylphosphatidylinositol (GPI) in sperm membrane.

Application

Angiotensin converting enzyme from rabbit lung has been used:
  • for measuring inhibitory effect of egg white protein hydrolysates on ACE activity by high performance liquid chromatography (HPLC)
  • to measure the ACE inhibition by litchi pericarp and cooked chicken breast using hippuryl-L-histidyl-L-leucine (HHL) as substrate by reverse phase-HPLC (RP-HPLC)3 and HPLC respectively
  • in releasing GPI anchored protein in vitro in few cell lines like HeLa, HEK293 and in vivo in mice sperm.

Biochem/physiol Actions

Removes C-terminal dipeptides from susceptible substrates, e.g., angiotensin I and bradykinin.

Quality

May contain traces of sodium chloride.

Unit Definition

One unit will produce 1.0 μmole of hippuric acid from Hippuryl-His-Leu per min in 50 mM HEPES and 300 mM NaCl at pH 8.3 at 37 °C.

Inhibitor

Product No.
Description
Pricing

Substrate

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

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)

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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Angiotensin-converting enzyme inhibitory activity of milk protein hydrolysates: Effect of substrate, enzyme and time of hydrolysis
Otte J, et al.
International dairy journal, 17(5), 488-503 (2007)
Angiotensin converting enzyme (ACE) inhibitory peptides derived from the simulated in vitro gastrointestinal digestion of cooked chicken breast
Sangsawad P, et al.
Journal of functional foods, 29, 77-83 (2017)
M Hernández-Presa et al.
Circulation, 95(6), 1532-1541 (1997-03-18)
The migration of monocytes into the vessel wall is a critical event leading to the development of atherosclerosis. Monocyte chemoattractant protein-1 (MCP-1) is the main chemotactic factor involved in this phenomenon, and nuclear factor-kappa B (NF-kappa B) is one of
Mina Ojaghi et al.
Molecular reproduction and development, 84(5), 376-388 (2017-03-01)
We hypothesized that the testis-specific isoform of angiotensin-converting enzyme (tACE) is released during bovine sperm capacitation, and its peptidase activity is required for capacitation. Specific objectives of this study were to (i) develop an anti-tACE antibody; (ii) characterize expression of
Enrichment and biotransformation of phenolic compounds from litchi pericarps with angiotensin I-converting enzyme (ACE) inhibition activity
Kessy HNE, et al.
LWT--Food Science and Technology, 87, 301-309 (2018)

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