A comparative study on bovine alpha-lactalbumin and lysozyme by nanosecond fluorometry.
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.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003619:Dansyl Compounds; D005450:Fluorescamine; D007768:Lactalbumin; D008433:Mathematics; D009113:Muramidase; D011485:Protein Binding; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013997:Time Factors
D003619:Dansyl Compounds; D005450:Fluorescamine; D007768:Lactalbumin; D009113:Muramidase