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51307-68-7

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51307-68-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 51307-68-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,1,3,0 and 7 respectively; the second part has 2 digits, 6 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 51307-68:
(7*5)+(6*1)+(5*3)+(4*0)+(3*7)+(2*6)+(1*8)=97
97 % 10 = 7
So 51307-68-7 is a valid CAS Registry Number.

51307-68-7Relevant articles and documents

Highly enantioselective intermolecular hydroamination of allylic amines with chiral aldehydes as tethering catalysts

MacDonald, Melissa J.,Hesp, Colin R.,Schipper, Derek J.,Pesant, Marc,Beauchemin, André M.

supporting information, p. 2597 - 2601 (2013/03/14)

Chirally LinkedIn: Chiral aldehydes are effective tethering catalysts for enantioselective intermolecular hydroamination, which provides access to vicinal diamine motifs in good yields and excellent enantioselectivities (see scheme). This work highlights simple chiral α-oxygenated aldehydes as effective organocatalysts capable of efficiently inducing asymmetry through transient intramolecularity. Copyright

A novel one-pot reductive amination of aldehydes and ketones with lithium perchlorate and zirconium borohydride-piperazine complexes

Heydari, Akbar,Khaksar, Samad,Esfandyari, Maryam,Tajbakhsh, Mahmoud

, p. 3363 - 3366 (2007/10/03)

A novel, one-pot reductive mono-alkylation method of amines (primary and secondary), 1,2-phenylenediamine, O-trimethylsilylhydroxylamine, and N,N-dimethylhydrazine was developed using LiClO4 (5 mol %) as a source for in situ generation of imine

Synthesis and tyrosinase inhibitory activity of novel N-hydroxybenzyl-N-nitrosohydroxylamines

Shiino, Mitsuhiro,Watanabe, Yumi,Umezawa, Kazuo

, p. 129 - 135 (2007/10/03)

Several novel N-substituted N-nitrosohydroxylamines were synthesized. They all inhibited mushroom tyrosinase, but the type of inhibition was different depending on the substituent. Some N-(mono- or dihydroxybenzyl)-N-nitrosohydroxylamines exhibited uncompetitive inhibition with respect to L-dopa. Among them, compound 6 was also a competitive inhibitor with respect to oxygen. This observation suggests that another interaction by the meta- or para-hydroxyl group might stabilize the binding of the inhibitor to the enzyme through the oxygen binding site.

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