Abstract
The interaction of acridine orange (C.I. Basic Orange 14) with bovine serum albumin and the subsequent sonodynamic damage to bovine serum albumin imparted by ultrasonic irradiation were studied. The quenching constant, binding constant and the binding site number were measured using fluorescence quenching. The distance of binding between the dye and the serum albumin was obtained according to Föster's nonradiative energy transfer theory. The effects of ultrasonic irradiation time, dye concentration, pH and ionic strength on bovine serum albumin were determined using UV–vis and fluorescence spectra; the extent of damage was enhanced by a increases in irradiation time, dye concentration and ionic strength, but was reduced by an increase in pH.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
