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• W2022791246 abstract "Polarization of fluorescence measurements on fluorescent conjugates of bovine α-lactalbumin and hen's egg white lysozyme indicate a difference in the rate of rotational diffusion of these two proteins. The rotational relaxation time measured for lysozyme was 25 nsec ±3 nsec and that measured for α-lactalbumin was 35 nsec ± 2 nsec. These data suggest that the effective molecular volume of α-lactalbumin in solution is larger than that of lysozyme. Since the molecular weight of these proteins is known to be the same (i.e., within 1%) from amino acid composition and sequence data, this behavior must be attributed to differences in conformation and hydration. The fluorescence lifetime of the dimethylaminonaphthalene sulfonate moiety has been measured directly in the case of each of these protein conjugates and the large difference in the values obtained illustrates the necessity of direct lifetime measurements whenever a new protein conjugate is prepared." @default.
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• W2022791246 date "1972-07-01" @default.
• W2022791246 modified "2023-10-11" @default.
• W2022791246 title "The rotational diffusion of bovine α-lactalbumin: A comparison with egg white lysozyme" @default.
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• W2022791246 doi "https://doi.org/10.1016/0003-9861(72)90467-5" @default.
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