title: Interaction of riboflavin binding protein with riboflavin, quinacrine, chlorpromazine and daunomycin.
abstract: 1. circular dichroism and fluorescence measurements were used to study the reversible unfolding of riboflavin-riboflavin binding protein complex. Both methods showed that the complex was unfolded according to the two-state model. 2. The results suggest that riboflavin was strongly bound in the hydrophobic cleft of the protein and that it could not be dislodged by TFE, MeOH or SDS without major unfolding of the unique tertiary structure of the protein. 3. In addition, it has been also shown that quinacrine, chlorpromazine and daunomycin did not form stereospecific complexes with riboflavin binding protein.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
authors.forename: A
authors.initials: A
authors.lastname: Galat
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism*; D002746:Chlorpromazine / Q000378:metabolism*; D002942:Circular Dichroism; D003630:Daunorubicin / Q000378:metabolism*; D005453:Fluorescence; D008433:Mathematics; D026901:Membrane Transport Proteins; D011796:Quinacrine / Q000378:metabolism*; D012256:Riboflavin / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D011796:Quinacrine; D012256:Riboflavin; D002746:Chlorpromazine; D003630:Daunorubicin