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THE EFFECT OF PSORALENS AND ANGELICINS ON PROTEINS IN THE PRESENCE OF UV‐A IRRADIATION
Author(s) -
Veronese F. M.,
Schiavon O.,
Bevilacqua R.,
Bordin F.,
Rodighiero G.
Publication year - 1981
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1981.tb09008.x
Subject(s) - irradiation , chemistry , ultraviolet irradiation , biophysics , food science , biology , physics , nuclear physics
— The photobinding to proteins of furocoumarins with linear and angular structure (psoralens and angelicins) has been found to occur at relatively high fluences of UV‐A irradiation (66.5 kJm 2 ). The extent of photobinding between serum albumin and the investigated furocoumarins (psoralen, 8‐methylpsoralen, 8‐methoxypsoralen, angelicin and 4,5′‐dimethylangelicin) varies largely with the furocoumarin structure and is correlated with the extent of photodegradation of the same furocoumarins when irradiated alone in aqueous solution. On the other hand, for each furocoumarin, the extent of photobinding varies considerably with different proteins.