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- W1473461212 endingPage "515" @default.
- W1473461212 startingPage "481" @default.
- W1473461212 abstract "Photoreactivating enzymes (PRE) or photolyases catalyze the light (300–600 nm)-dependent monomerization of cyclobutyl pyrimidine dimers, formed between adjacent pyrimidines on the same DNA strand, upon exposure to ultraviolent (UV) irradiation (220–320 nm). Biological photoreactivation and photoreactivating enzymes are ubiquitous. Photoreactivating enzyme levels are regulated within an organism, so PRE activity may vary from tissue to tissue within an organism, for different growth stages of a culture, according to the developmental stage of the organism, or for the same cells in different culture conditions. In addition to the presence of an intact photoreactivating enzyme in a suitable buffer with a dimer-containing DNA substrate, the photoreactivation reaction has a unique second requirement-light. Photoreactivating enzyme function by absorbing light in the range 300–600 nm, the exact maximum and range varying between the different enzymes. Further, the reaction has a temporal requirement; the enzyme must be associated with the first substrate, the dimer in DNA, before the absorption of the photon can occur and thus drive the photocatalysis of the dimer monomerization. Photoreactivation has been measured chiefly by three methods—namely, (1) the transformation assay, (2) direct measurement of pyrimidine dimer content in the DNA before and after photoreactivation, and (3) nuclease-digestion assay." @default.
- W1473461212 created "2016-06-24" @default.
- W1473461212 creator A5079110185 @default.
- W1473461212 date "1981-01-01" @default.
- W1473461212 modified "2023-09-27" @default.
- W1473461212 title "24 Photoreactivating Enzymes" @default.
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