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Photochemical reactions of fentichlor with soluble proteins


Chemico-Biological Interactions 52(2): 213-222
Photochemical reactions of fentichlor with soluble proteins
The photochemical reactions of the photoallergen fetichlor with soluble proteins have been studied. [35S] fentichlor bound covalently to human serum albumin (HSA) when irradiated with UV light (313 nm). HSA had the ability to bind at least 8 molecules of fentichlor/molecule protein. Fractionation of fentichlor-HSA photoadducts after treatment with cyanogen bromide and reduction, carboxymethylation and digestion with trypsin showed that the bound fentichlor was distributed evenly throughout the sequence of the HSA molecule. Fentichlor also formed photoadducts with human .gamma.-globulin and with bovine insulin. Its binding to insulin was restricted to the B chain of the molecule. Fundamental differences between the photochemical reactions of the photoallergens fentichlor and tetrachlorosalicylanilide (T4CS) with soluble proteins were discussed. The reactions of fentichlor with soluble proteins were not restricted to specific binding sites (unlike T4CS). Fentichlor had the potential to react photochemically with a wide range of proteins in the epidermis and dermis, to form antigens.

Accession: 006110180

PMID: 6210158

DOI: 10.1016/0009-2797(84)90074-7

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Related references

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