A comparative study on bovine alpha-lactalbumin and lysozyme by nanosecond fluorometry. |
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Authors: | L H Tang Y Kubota R F Steiner |
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Affiliation: | Department of Chemistry, University of Maryland, Baltimore County, Baltimore, Maryland 21228, USA |
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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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