PMID:6363715
Citation |
Sancar, A and Sancar, GB (1984) Escherichia coli DNA photolyase is a flavoprotein. J. Mol. Biol. 172:223-7 |
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Abstract |
Escherichia coli DNA photolyase (photoreactivating enzyme) was purified to homogeneity from a strain that greatly overproduces the protein. The purified enzyme has absorption peaks at 280 and 380 nm, a fluorescence emission peak at 480 nm and, upon denaturation, releases a chromophore that has the spectroscopic properties of flavin adenine dinucleotide (FAD), indicating that FAD is an intrinsic chromophore of the enzyme. |
Links | |
Keywords |
DNA Repair/drug effects; Deoxyribodipyrimidine Photo-Lyase/isolation & purification; Deoxyribodipyrimidine Photo-Lyase/pharmacology; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Flavoproteins/isolation & purification; Lyases/isolation & purification; Spectrometry, Fluorescence |
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