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- W1964187558 abstract "The luminescence of bovine α-lactalbumin at 77 K has been studied and compared with that of lysozyme. α-Lactalbumin has several unusual properties, including a fluorescence spectrum showing vibrational fine structure, an abnormal phosphorescence spectrum, a high fluorescence: phosphorescence ratio and an abnormal phosphorescence decay. These properties are largely due to the proximity of tryptophan residues to disulphide bonds. Reduction of all these bonds causes considerable changes in α-lactalbumin luminescence, as does denaturation in acid solution. Reduction of a single labile disulphide bond has little effect, and the properties of α-lactalbumin III, a variant lacking one disulphide bond and one tryptophan residue, are similar to those of the normal protein. Several differences between α-lactalbumin and lysozyme are reported. The results support the suggestion that the two tryptophan residues found in the active site cleft of α-lactalbumin may be largely responsible for its luminescence." @default.
- W1964187558 created "2016-06-24" @default.
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- W1964187558 date "1975-06-01" @default.
- W1964187558 modified "2023-10-10" @default.
- W1964187558 title "The low-temperature luminescence properties of bovine α-lactalbumin" @default.
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- W1964187558 doi "https://doi.org/10.1016/0005-2795(75)90072-0" @default.
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