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A comparative study on bovine alpha-lactalbumin and lysozyme by nanosecond fluorometry.
Authors:L H Tang  Y Kubota  R F Steiner
Affiliation:Department of Chemistry, University of Maryland, Baltimore County, Baltimore, Maryland 21228, USA
Abstract:Analysis of the time decay of fluorescence anisotropy of 1-dimethylaminoaphthalene-5-sulfonyl (DNS) and fluorescamine derivatives of bovine alpha-lactalbumin and lysozyme reveals that no significant differences in mean rotational relaxation times are present. While fluorescamine molecules appear to orient randomly on these proteins, DNS is bound with a preferential orientation. Other fluorescence characteristics of the labels are also cited.
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