A2580
Angiotensin Converting Enzyme from porcine kidney
lyophilized powder, ≥10 units/mg protein (Bradford)
Synonym(s):
ACE, Peptidyl-dipeptidase A
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352200
NACRES:
NA.32
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form
lyophilized powder
Quality Level
specific activity
≥10 units/mg protein (Bradford)
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
pig ... ACE(613133)
Related Categories
General description
ACE is a monomer with molecular weight of ~170 kDa
pH range for activity: 7-8.5
Temperature optimum: 37 °C
Zinc is required for activity
Inhibitors: captopril, enalaprilat, lisinopril etc. (1-10 μM)
pH range for activity: 7-8.5
Temperature optimum: 37 °C
Zinc is required for activity
Inhibitors: captopril, enalaprilat, lisinopril etc. (1-10 μM)
Angiotensin converting enzyme (ACE) is encoded by the gene, mRNA-decapping enzyme subunit 1 (DCP1). It is a zinc metalloprotease, which belongs to the M2 family.
Application
Angiotensin converting enzyme from porcine kidney has been used in in vitro angiotensin-converting enzyme (ACE) inhibition assay.
Biochem/physiol Actions
Angiotensin converting enzyme (ACE) catalyzes the conversion of angiotensin I to angiotensin II, which regulates the fluid-electrolyte balance and systemic blood pressure. ACE inhibits the vasodilator, bradykinin. ACE inhibitors are used to treat high blood pressure.
Removes C-terminal dipeptides from susceptible substrates, e.g., angiotensin I and bradykinin.
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.
Physical form
Lyophilized powder containing Tris buffer salts.
inhibitor
Product No.
Description
Pricing
substrate
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
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
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A Human Homolog of Angiotensin Converting Enzyme-Cloning and Functional Expression As A Captopril Insensitive Carboxypeptidase
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The Journal of Biological Chemistry (2000)
Sequence variation in the human angiotensin converting enzyme
Rieder MJ, et al.
Nature Genetics, 22(1), 59-59 (1999)
N M Hooper et al.
The Biochemical journal, 241(3), 625-633 (1987-02-01)
Peptidyl-dipeptidase A (angiotensin converting enzyme; ACE, EC 3.4.15.1), has been purified from pig kidney and striatum by affinity chromatography employing the selective inhibitor lisinopril as ligand. The inclusion of a 2.8 nm spacer arm improved the yield of the enzyme
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Lokesh D and Amitsankar D
Journal of Ethnopharmacology, 143(1), 207-212 (2012)
Effect of angiotensin-converting-enzyme inhibition compared with conventional therapy on cardiovascular morbidity and mortality in hypertension: the Captopril Prevention Project (CAPPP) randomised trial
Hansson L, et al.
Lancet, 353(9153), 611-616 (1999)
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