Abstract— 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 kJm2). 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. Copyright © 1981, Wiley Blackwell. All rights reserved
The effect of psoralens and angelicins on proteins in the presence of UV-A irradiation.
SCHIAVON, ODDONE;
1981
Abstract
Abstract— 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 kJm2). 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. Copyright © 1981, Wiley Blackwell. All rights reservedPubblicazioni consigliate
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