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- W1559625990 abstract "The technique of fluorescence polarization was used to study the rotational mobility of pyridoxyl 5-phosphate covalently bound to the e-amino group of a lysine residue. A Perrin's plot of the polarization of fluorescence data obtained by varying the viscosity of the solution shows a downward curvature at T/η values lower than 104. Two rotational relaxation times (ρs = 0.16 nsec) and (ρh = 8.7 nsec) are needed to fit the experimental curve. Both rotational relaxation times are shorter than the value (ρh = 25 nsec) obtained for lysozyme tagged with fluorescein isothiocyanate; they do not correlate with the value expected (ρh = 20 nsec) for the equivalent hydrated sphere of 14,500 molecular weight. A comparison between the rotational relaxation times of pyridoxyl 5-phosphate lysozyme, pyridoxyl-lysine, and the pyridoxyl 5-phosphate peptide reveals that the shortest rotational relaxation time (ρs = 0.16 nsec) of lysozyme reflects the motion of the pyridoxyl 5-phosphate chromophore linked the e-amino group of lysine. The effect of tri-N-acetylglucosamine on the degree of polarization of fluorescence of lysozyme was examined over a wide range of temperatures. The results of these studies indicate that the polarized fluorescence emitted by pyridoxyl 5-phosphate is influenced by events occurring at the level of the polypeptide chain." @default.
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- W1559625990 date "1971-09-01" @default.
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- W1559625990 title "Rotational Relaxation Time of Pyridoxyl 5-Phosphate Lysozyme" @default.
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- W1559625990 doi "https://doi.org/10.1016/s0021-9258(18)61910-6" @default.
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