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About This Item
Empirical Formula (Hill Notation):
C20H21N3O6
CAS Number:
Molecular Weight:
399.40
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.32
MDL number:
Product Name
N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly,
Quality Level
storage temp.
−20°C
SMILES string
OC(=O)CNC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)\C=C\c2ccco2
InChI
1S/C20H21N3O6/c24-17(9-8-15-7-4-10-29-15)23-16(11-14-5-2-1-3-6-14)20(28)22-12-18(25)21-13-19(26)27/h1-10,16H,11-13H2,(H,21,25)(H,22,28)(H,23,24)(H,26,27)/b9-8+/t16-/m0/s1
InChI key
ZDLZKMDMBBMJLI-FDMDGMSGSA-N
Gene Information
human ... ACE(1636), ACE2(59272)
mouse ... ACE3(217246)
rat ... ACE(11421), ACE2(70008), ACE3(498012)
General description
A substrate for continuous spectrophotometric assay of angiotensin converting enzyme (ACE).
N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly acts as a substrate for angiotensin converting enzyme (ACE), and is used in inhibitory assays of ACE.
Application
N-[3-(2-Furyl)acryloyl]-Phe-Gly-Gly has been used for kinetic spectrophotometric assay of ACE (angiotensin converting enzyme) inhibitory activity.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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J E Buttery et al.
Clinical chemistry, 39(2), 312-316 (1993-02-01)
In the kinetic angiotensin-converting enzyme (ACE) method, a practical and optimal buffer is 80 mmol/L borate buffer at pH 8.2 (37 degrees C). A lag phase is detected in the reaction, and a 5-min incubation of substrate and plasma is
Wen-Chi Hou et al.
Journal of agricultural and food chemistry, 51(6), 1706-1709 (2003-03-06)
Five commercial peptides, namely, reduced glutathione (GSH), oxidized glutathione (GSSG), carnosine, homocarnosine, and anserine, were used to test angiotensin converting enzyme inhibitory (ACEI) activities using N-[3-(2-furyl)acryloyl]-Phe-Gly-Gly (FAPGG) as a substrate. All of these peptides showed dose-dependent ACEI activities. Using 50%
Siqi Sun et al.
Marine drugs, 17(3) (2019-03-22)
Angiotensin I-converting enzyme (ACE) inhibitory peptides derived from seaweed represent a potential source of new antihypertensive. The aim of this study was to isolate and purify ACE inhibitory peptides (ACEIPs) from the protein hydrolysate of the marine macroalga Ulva intestinalis.