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C48H32F6N4O2P(1+)*Cl(1-) is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

173681-45-3

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173681-45-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 173681-45-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,7,3,6,8 and 1 respectively; the second part has 2 digits, 4 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 173681-45:
(8*1)+(7*7)+(6*3)+(5*6)+(4*8)+(3*1)+(2*4)+(1*5)=153
153 % 10 = 3
So 173681-45-3 is a valid CAS Registry Number.

173681-45-3Upstream product

173681-45-3Downstream Products

173681-45-3Relevant articles and documents

Photosensitized damage of protein by fluorinated diethoxyphosphorus(V) porphyrin

Hirakawa, Kazutaka,Azumi, Keito,Nishimura, Yoshinobu,Arai, Tatsuo,Nosaka, Yoshio,Okazaki, Segetoshi

, p. 56 - 62 (2013)

The effect of the axial ligand fluorination of the water-soluble P(V)porphyrin complex on photosensitized protein damage was examined. The activity of singlet oxygen generation by diethoxyP(V) porphyrin was slightly improved by the fluorination of the ethoxy chains. Absorption spectrum measurements demonstrated the binding interaction between the P(V)porphyrins and human serum albumin, a water-soluble protein. Photo-irradiated P(V)porphyrins damaged the amino acid residue of human serum albumin, resulting in the decrease of the fluorescence intensity from the tryptophan residue of human serum albumin. A singlet oxygen quencher, sodium azide, could not completely inhibit the damage of human serum albumin, suggesting that the electron transfer mechanism contributes to protein damage as does singlet oxygen generation. The decrease of the fluorescence lifetime of P(V)porphyrin by human serum albumin supported the electron transfer mechanism. The estimated contributions of the electron transfer mechanism are 0.57 and 0.44 for the fluorinated and non-fluorinated P(V)porphyrins, respectively. The total quantum yield of the protein photo-oxidation was slightly enhanced by this axial fluorination. Copyright

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