THE EFFECT OF PSORALENS AND ANGELICINS ON PROTEINS IN THE PRESENCE OF UV‐A IRRADIATION
THE EFFECT OF PSORALENS AND ANGELICINS ON PROTEINS IN THE PRESENCE OF UV‐A IRRADIATION
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UV-A 照射下补骨脂素和当归素对蛋白质的影响
DOI：
10.1111/j.1751-1097.1981.tb09008.x
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发表时间：
1981
影响因子：
3.3
通讯作者：
G. Rodighiero
中科院分区：
文献类型：
--
作者：
F. Veronese;O. Schiavon;R. Bevilacqua;F. Bordin;G. Rodighiero
摘要-已发现具有线性和角结构的呋喃香豆素（peptiens和angelicins）与蛋白质的光结合发生在相对高的UV-A辐射通量（66.5 kJm 2）下。血清白蛋白与所研究的呋喃香豆素类化合物（补骨脂素、8-甲基补骨脂素、8-甲氧基补骨脂素、当归素和4，5 ′-二甲基当归素）之间的光结合程度随呋喃香豆素的结构而变化很大，并且与在水溶液中单独照射时相同呋喃香豆素类化合物的光降解程度相关。另一方面，对于每种呋喃香豆素，光结合的程度随不同的蛋白质而变化很大。
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.