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4-<(7-chloro-4-quinolinyl)amino>-2-<(dietyhlamino)methyl>phenol 1-oxide is a complex organic compound with a molecular formula of C23H26ClN3O2. It is characterized by a phenol core, which is substituted with a 7-chloro-4-quinolinyl group at the 4-position and a diethylaminomethyl group at the 2-position. The 1-oxide functional group indicates the presence of an oxygen atom that is covalently bonded to the phenol ring, which can influence the compound's reactivity and properties. This chemical structure suggests potential applications in pharmaceuticals or as a chemical intermediate, given the presence of a quinoline ring and a phenol group, which are common in various biologically active compounds. However, without specific context or application, it is difficult to provide a more detailed summary of its uses or properties.

1245-26-7

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1245-26-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1245-26-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 1,2,4 and 5 respectively; the second part has 2 digits, 2 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 1245-26:
(6*1)+(5*2)+(4*4)+(3*5)+(2*2)+(1*6)=57
57 % 10 = 7
So 1245-26-7 is a valid CAS Registry Number.

1245-26-7Downstream Products

1245-26-7Relevant academic research and scientific papers

Anticholinesterase activity of 4-aminoquinolines related to amodiaquine and their respective N-oxides

Go,Ngiam,Lim

, p. 81 - 85 (2007/10/02)

The inhibitory activities of a series of substituted 4-aminoquinolines related to the antimalarial agent amodiaquine and their respective N-oxides toward acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) have been determined and discussed in terms of their proposed mode of interaction with the enzyme surface. A marked difference was noted in the AChE and BChE inhibitory potencies of these compounds. The strong anti-AChE activity of amodiaquine has been explained by a specific two-point interaction with the anionic site and acidic group of AChE. However, such an interaction appears to be absent in the case of the amodiaquine inhibition of BChE, suggesting differences in the ability of the enzymes to accommodate similar inhibitory molecules.

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