On the Addition of Protons to Derivatives of 4-Aminoazobenzene<sup>1</sup>

Cilento, Giuseppe; Miller, E. C.; Miller, J. A.

doi:10.1021/ja01589a065

Cited by 37 publications

(13 citation statements)

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“…[1] Upon continuous irradiation of the πǞπ* transition, AB reaches a photostationary state consisting of 1:9 trans/cis isomers. [36,37] Whereas, like AB, aminoABs undergo transǞcis isomerization when irradiated, thermal cisǞtrans isomerization occurs quickly within minutes or hours. Thermal relaxation of cis-AB has a halflife (t 1/2 ) of several days.…”

Section: Resultsmentioning

confidence: 99%

“…In aminoABs, the πǞπ* transition shifts to higher wavelengths and overlaps the nǞπ* transition. [36,37] Whereas, like AB, aminoABs undergo transǞcis isomerization when irradiated, thermal cisǞtrans isomerization occurs quickly within minutes or hours. [35] As a result, accurately determining the trans/cis ratio at the photostationary state can be difficult.…”

Section: Photochemistry Of Azobenzene Aminoazobenzenes and Azoamp-1mentioning

confidence: 99%

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Systematic Modulation of Hydrogen Bond Donors in Aminoazobenzene Derivatives Provides Further Evidence for the Concerted Inversion Photoisomerization Pathway

et al. 2013

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A series of aminoazobenzene derivatives structurally related to AzoAMP‐1 have been prepared and characterized by using a variety of analytical techniques. AzoAMP‐1 is based on 2,2′‐diaminoazobenzene with N‐methylpyridine groups. The new derivatives all contain a hydrogen bond between the aniline hydrogen atom and the azo group, as well as a separate pendant functional group that could contribute an additional hydrogen‐bond acceptor to an intramolecular network. A combination of photoisomerization studies and NMR spectroscopic and X‐ray crystallographic investigations suggest that AzoAMP‐1 possesses a unique structure that prevents isomerization through the concerted inversion pathway, which cannot be reproduced with other types or arrangements of substituents. Only AzoAMQ, which contains a similar quinolone heterocycle in place of the pyridine group of AzoAMP‐1, displayed somewhat similar photochemistry.

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Section: Resultsmentioning

confidence: 99%

Section: Photochemistry Of Azobenzene Aminoazobenzenes and Azoamp-1mentioning

confidence: 99%

Systematic Modulation of Hydrogen Bond Donors in Aminoazobenzene Derivatives Provides Further Evidence for the Concerted Inversion Photoisomerization Pathway

et al. 2013

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“…After slicing, the gels were soaked first in 5% (wfv) trichloroacetic acid in 50% (v/v) ethanol to show the position of bound azo-dye, which in strong acid occurs largely as the red azonium ion (Cilento, Miller & Miller, 1956), and then in a nigrosine stain to show the position of the protein. The nigrosine stain consisted of 1-0g.…”

Section: Starch-gel Electrophoreai8mentioning

confidence: 99%

The isolation of carcinogen-binding protein from livers of rats given 4-dimethylaminoazobenzene

Ketterer¹,

Ross-Mansell²,

Whitehead³

1967

Biochemical Journal

157

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1. Three azo-dye-binding proteins were identified in the soluble cell supernatant fraction from livers of rats that had received 4-dimethylaminoazobenzene by intraperitoneal injection. 2. One is basic and was highly purified. It has an isoelectric point of pH8.4 in barbital-sodium chloride buffer, I0.1, an S(20,w) value of 3.5s and a molecular weight determined by Sephadex chromatography of 45000. 3. It does not have N-terminal amino acids with free alpha-amino groups. 4. Digestion with Pronase gives rise to a single azo-dye-bound peptide, which on hydrolysis is shown to contain glycine, alanine, serine, threonine, glutamic acid and aspartic acid. The amino acid that binds the azo-dye was not identified. 5. On starch-gel electrophoresis the basic protein separates into a double band, indicating microheterogeneity. 6. The other two proteins were partially purified and occur in a fraction together. They have isoelectric points near neutrality and a molecular weight as determined by Sephadex chromatography of 13800. 7. The absorption spectra in formic acid of both the basic and the low-molecular-weight proteins are similar. The azonium ion has an absorption maximum at 518mmu and another adsorbed chromogen is present with an absorption maximum at 395mmu.

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“…It is, therefore, not possible to calculate the number of moles of the various dyes bound per unit weight of protein from the optical density. The molecular extinction coefficients of the original pure dyes differ widely (Table I; see also Miller, Sapp and Miller, 1948;and Cilento, Miller and Miller, 1956) owing largely to differences in the ratio of azonium (-N+H-N-) to ammonium (-N+HMe2) tantomers, of which the ratio E520/E325 gives a rough measure (Sawicki, 1957). For example, under the conditions of measurement used in the present paper, 3'-MeDAB and 2'-MeDAB had molecular extinction coefficients at 520 m/t of 44,400 and 10,400, and E520/E325 ratios of 5 and 0*6 respectively.…”

Section: Resultsmentioning

confidence: 99%

“…Sawicki (1957) found that the molecular extinction coefficients at 520 m,t of some dyes with an unsubstituted amino group were several times smaller than the molecular extinction coefficients of their monomethylamino and their dimethylamino derivatives. Since N-demethylation is one of the major metabolic reactions of aminoazo dyes in the body (Miller and Miller, 1953;Conney et al, 1957;Matsumoto and Terayama, 1961), this is another factor which may influence the extinction coefficients of the bound dyes. As pointed out by Dijkstra and Joubert (1961), the difference in the wavelengths of maximum absorption of the dye bound to liver and serum proteins of the same rat may be a reflection of a difference in the extent of N-demethylation in these two cases.…”

Section: Resultsmentioning

confidence: 99%

Protein-Bound Dyes in the Serum and Liver of Rats Fed Aminoazo Dyes

Dijkstra¹,

Louw²

1962

Br J Cancer

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IT was previously reported (Dijkstra and Joubert, 1961) that the albumin fraction isolated from serum of rats fed a single dose of the carcinogen 3'-methyl-4-dimethylaminoazobenzene contained significant quantities of protein-bound dye, which was only released by prolonged hydrolysis of the protein. The present work reports observations on the relative importance of dye binding to liver and serum proteins after administration of various aminoazo dyes of different degrees of carcinogenicity. MATERIALS AND METHODSReagents. Treatment of animals.-Male albino rats (weight 180-220 g.) of the Wistar strain were fasted for 6 hours before the administration by stomach tube of 50 mg. of aminoazo dye in 2 ml. of olive oil. After dosing, the animals were fed ad libitum on stock diet (Dijkstra and Joubert, 1961) and tap water. At intervals the rats were anaesthetized with ether, the abdominal cavity was exposed and the blood was obtained from the abdominal aorta. The liver was immediately perfused in situ with cold 2 per cent sodium citrate (Miller and Miller, 1947).Estimation of dye.-Free (i.e. alcohol-extractable) dye and the protein-bound dye were determined (Dijkstra and Joubert, 1961) in the serum after precipitation of proteins with 50 ml. of absolute ethyl alcohol per 2 ml. of serum, and in the liver after homogenization of the left lateral lobe (2-3 g.) in 50 ml. of absolute ethyl alcohol. The optical absorption of the dye was measured at 520 m#t and it was ascertained that this involved no appreciable error in cases where the wavelength of maximum absorption differed from 520 m,u. The results of the bound dye determinations are expressed as the optical density (E) at 520 m, by the dye from 50 mg. of protein in a mixture of 2-0 ml. of ethyl alcohol and 2-5 ml. of 7 N hydrochloric acid using an absorption cell with a light path of 1 cm. (Miller and Miller, 1947). The results of the free dye estimations are similarly expressed, using the mean values of 7 0 and 20-0 per cent for the protein content in the serum and the liver respectively.The absorption spectra of the bound dyes from liver and serum were obtained as previously reported (Dijkstra and Joubert, 1961) at 38 hours after dye ad-

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On the Addition of Protons to Derivatives of 4-Aminoazobenzene¹

Cited by 37 publications

References 2 publications

Systematic Modulation of Hydrogen Bond Donors in Aminoazobenzene Derivatives Provides Further Evidence for the Concerted Inversion Photoisomerization Pathway

Systematic Modulation of Hydrogen Bond Donors in Aminoazobenzene Derivatives Provides Further Evidence for the Concerted Inversion Photoisomerization Pathway

The isolation of carcinogen-binding protein from livers of rats given 4-dimethylaminoazobenzene

Protein-Bound Dyes in the Serum and Liver of Rats Fed Aminoazo Dyes

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On the Addition of Protons to Derivatives of 4-Aminoazobenzene1

Cited by 37 publications

References 2 publications

Systematic Modulation of Hydrogen Bond Donors in Aminoazobenzene Derivatives Provides Further Evidence for the Concerted Inversion Photoisomerization Pathway

Systematic Modulation of Hydrogen Bond Donors in Aminoazobenzene Derivatives Provides Further Evidence for the Concerted Inversion Photoisomerization Pathway

The isolation of carcinogen-binding protein from livers of rats given 4-dimethylaminoazobenzene

Protein-Bound Dyes in the Serum and Liver of Rats Fed Aminoazo Dyes

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On the Addition of Protons to Derivatives of 4-Aminoazobenzene¹