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DYE‐SENSITIZED PHOTOÖXIDATION OF OVALBUMIN *
Author(s) -
Bellin Judith S.,
Entner Gail
Publication year - 1966
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.1751-1097.1966.tb05788.x
Subject(s) - chemistry , ovalbumin , photochemistry , thionine , photodegradation , denaturation (fissile materials) , substrate (aquarium) , isoelectric point , radical , proflavine , organic chemistry , electrochemistry , nuclear chemistry , biochemistry , enzyme , dna , oceanography , immune system , electrode , photocatalysis , immunology , biology , geology , catalysis
— The dye‐sensitized photodegradation of ovalbumin is shown to involve the reduction of light‐excited dye molecules by the substrate. The photodynamic denaturation of ovalbumin, therefore, results both from attack by ‘dye‐peroxide’ molecules (as is the case when the substrate can not act as a photoreductant) and from attack by OH radicals which are generated by re‐oxidation in the dark of the photoreduced dye molecules. Cysteine, histidine, methionhe, tyrosineand tryptophan can act as photoreductants formethylene blue, thionine and proflavine. Photodynamic denaturation of ovalbumin results in a decrease in solubility of the protein at its isoelectric point, and changes its immunological reactivity.