1. Studies on the protein binding mechanism of p-aninodiphenylamine: A hair dye constituent
- Author
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G.B. Singh, Subhash K. Khanna, Laj Srivastava, and C.R. Krishna Murti
- Subjects
Environmental Engineering ,Health, Toxicology and Mutagenesis ,Binding protein ,Public Health, Environmental and Occupational Health ,General Medicine ,General Chemistry ,Plasma protein binding ,Pollution ,Protein chain ,Quinone ,Ion ,chemistry.chemical_compound ,chemistry ,Hair dyes ,Aspartic acid ,Polymer chemistry ,Environmental Chemistry ,Organic chemistry ,Derivative (chemistry) - Abstract
p-Aminodiphenylamine (p-ADPA) has got a binding capacity with tissue proteins. Aspartic and glutamic acids are presumably the responsible units in the protein chain involved in this binding with p-ADPA. p-ADPA is changed into a quinone structure after atmospheric oxidation in Krebs-Ringer-Bicarbonate buffer, pH 7.4 in the presence of trace metal ions. This oxidised form of p-ADPA binds with aspartic acid at pH 7.4 and temperature 40° in 2 hrs. The derivative thus formed absorbs at 450 nm instead of 430 nm.
- Published
- 1982