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18537-00-3

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18537-00-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 18537-00-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,8,5,3 and 7 respectively; the second part has 2 digits, 0 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 18537-00:
(7*1)+(6*8)+(5*5)+(4*3)+(3*7)+(2*0)+(1*0)=113
113 % 10 = 3
So 18537-00-3 is a valid CAS Registry Number.

18537-00-3Downstream Products

18537-00-3Relevant articles and documents

Synthesis of colloidal Janus nanoparticles by asymmetric capping of mesoporous silica with phenylsilsesquioxane

Ujiie, Hiroto,Shimojima, Atsushi,Kuroda, Kazuyuki

supporting information, p. 3211 - 3214 (2015/06/03)

Colloidal mesoporous silica nanoparticles asymmetrically capped with non-porous phenylsilsesquioxane have been prepared by adding phenyltriethoxysilane to an aqueous dispersion of mesostructured silica-surfactant composite nanoparticles. The integration of colloidal stability, mesoporosity and the Janus structure is quite promising for materials design applicable in various fields, including catalysis, biomedicine and coatings.

The enzymatic cleavage of Si-O bonds: A kinetic analysis of the biocatalyzed hydrolysis of phenyltrimethoxysilane

Frampton, Mark B.,Simionescu, Razvan,Dudding, Travis,Zelisko, Paul M.

experimental part, p. 105 - 112 (2011/01/03)

Previously we reported the ability of trypsin to mediate the cross-linking of alkoxysily-functionalized silicone polymers. Although enzymes and silicon-containing compounds are not necessarily incompatible species, the exact mechanism of how enzymes process silicon substrates is not fully understood. The focus of this current work was to examine the reaction kinetics associated with the processing of an alkoxysilane substrate by enzymes using 29Si NMR so as to gain a greater insight into the actual reaction mechanism, especially those involving more complex silicone systems. A series of time course 29Si NMR experiments using D2O revealed that the trypsin-mediated hydrolysis of a single alkoxy moiety in water is a pseudo-first order reaction. The relative effect of the enzyme was determined to be β = 3.549 while the relative effect of water was γ = 3.325. Prolonged contact with phenyltrimethoxysilane was not sufficiently deleterious to the enzyme and did not induce the complete and irreversible denaturation of trypsin. Computational evidence suggests that while in the active site of the enzyme, serine addition to silicon to forms a pentacoordinate species and is favoured over histidine addition.

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