Srivastava, L. P. ; Khanna, S. K. ; Singh, G. B. ; Krishna Murti, C. R. (1982) Studies on the protein binding mechanism of p-aninodiphenylamine: a hair dye constituent Chemosphere, 11 (2). pp. 175-183. ISSN 0045-6535
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/004565...
Related URL: http://dx.doi.org/10.1016/0045-6535(82)90164-3
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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| ID Code: | 29386 |
| Deposited On: | 17 Dec 2010 08:08 |
| Last Modified: | 04 Jun 2011 09:09 |
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