Abstract
A fluorescent dye, 1-dimethylaminonaphthalene-5-sulfonyl chloride, was used to label bovine serum albumin (BSA), intact and disulfide bridges-cleaved. The fluorescence lifetime and fluorescence anisotropy of the adducts in sodium dodecyl sulfate (SDS) solutions were studied by the nanosecond fluorescence depolarization method. The volume of equivalent sphere (V e) was calculated to be 2.1×10−19 cm3 for BSA with the intact disulfide bridges from the rotational correlation time. The value ofV e was 4.4×10−19 cm3 for the disulfide bridges-cleaved BSA. With an increase in SDS concentration, the rotational correlation time of the intact BSA became longer, while that of the disulfide bridges-cleaved BSA became shorter. This suggests that upon the binding of SDS, the total volume of the intact BSA increases while the expanded state of the protein, caused by the cleavage of the disulfide bridges, becomes compact.
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Takeda, K., Yamamoto, K. Fluorescence lifetime and rotational correlation time of bovine serum albumin-sodium dodecyl sulfate complex labeled with 1-dimethylaminonaphthalene-5-sulfonyl chloride: Effect of disulfide bridges in the protein on these fluorescence parameters. J Protein Chem 9, 17–22 (1990). https://doi.org/10.1007/BF01024979
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DOI: https://doi.org/10.1007/BF01024979