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Quality Level
Assay
97%
form
solid
reaction suitability
reaction type: solution phase peptide synthesis
mp
261 °C (dec.) (lit.)
application(s)
peptide synthesis
SMILES string
NC1(CCC1)C(O)=O
InChI
1S/C5H9NO2/c6-5(4(7)8)2-1-3-5/h1-3,6H2,(H,7,8)
InChI key
FVTVMQPGKVHSEY-UHFFFAOYSA-N
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Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Oral - Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
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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Neuropharmacology, 29(8), 727-730 (1990-08-01)
In Xenopus oocytes, injected with mRNA from the brain of the rat, the characteristics of the cyclic homologues of glycine, ACPC, ACBC and cycloleucine have been examined. 1-Aminocyclopropane-1-carboxylate was a potent agonist at the NMDA-associated glycine site (EC50 = 0.09
Chemistry & biology, 5(1), 49-57 (1998-02-28)
The chemical mechanism of the final step of ethylene biosynthesis (the conversion of 1-aminocyclopropanecarboxylic acid, ACC, to ethylene by ACC oxidase, the ethylene-forming enzyme, EFE) is poorly understood. Two possibilities have been suggested: a radical mechanism and an N-hydroxylation mechanism.
Brain research bulletin, 32(3), 223-226 (1993-01-01)
Arachidonic acid [20:4(N-6)] has been implicated in neurological damage induced by cerebral ischaemia. Membrane arachidonate concentrations can be reduced by changes in dietary fat intake. Therefore, in the present study, we have investigated the effects of N-3 fatty acid supplementation
European journal of pharmacology, 167(2), 291-294 (1989-08-22)
ACBC has been reported to have the binding profile of an antagonist at the glycine site of the NMDA receptor. In Xenopus oocytes injected with rat brain mRNA, we have confirmed the antagonist action of ACBC on NMDA responses. ACBC
Plant & cell physiology, 38(3), 312-318 (1997-03-01)
We partially purified 1-aminocyclopropane-1-carboxylate (ACC) oxidase from senescing petals of carnation (Dianthus caryophyllus L. cv. Nora) flowers and investigated its general characteristics, and, in particular, the inhibition of its activity by ACC analogs. The enzyme had an optimum pH at
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