Spectroscopic probing of bile salt-albumin interaction.
Interaction of the bile salts, sodium cholate and sodium deoxy cholate with albumin has been probed by fluorescence and circular dichroism studies. Both covalently and non-covalently labeled protein have been used to follow the aggregation of bile salts in presence of protein and to study bile salt-protein interactions in general. Time resolved studies, in agreement with steady-state fluorescence and circular dichroism studies, indicate alteration of protein secondary structure due to positive co-operative effects in bile salt binding to protein. These studies also indicate that covalent labeling may not always be good for studying proteins as it causes alteration of protein secondary structure.
De
Swati
S
Department of Chemistry, University of Kalyani, Kalyani 741235, India. swati_de1@rediffmail.com
Das
Susmita
S
Girigoswami
Agnishwar
A
D000818:Animals; D001647:Bile Acids and Salts / Q000737:chemistry*; D001665:Binding Sites; D002417:Cattle; D002942:Circular Dichroism; D019793:Fluorescein / Q000737:chemistry; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
D001647:Bile Acids and Salts; D012710:Serum Albumin, Bovine; D019793:Fluorescein