Quantification of binding of some thiol-reactive clenbuterol analogues to bovine serum albumin by electron paramagnetic resonance spectroscopy.
The only free thiol group of bovine serum albumin (BSA) was coupled in a high yield with some novel thiol-reactive clenbuterol analogues. The unreacted cysteines were probed with maleimide spin label to determine the yield of the coupling reaction. A novel approach to determining free thiol groups of BSA quantitatively by electron paramagnetic resonance spectroscopy and spectral decomposition without the usual gel-filtration step or extensive dialysis is presented.
Prezelj
Andrej
A
Faculty of Pharmacy, University of Ljubljana, Ljubljana 1000, Slovenia. abdrej.prezelj@ffa.uni-lj.si
Strancar
Janez
J
Gubensek
Franc
F
Pecar
Slavko
S
Degand
Guy
G
D000818:Animals; D002417:Cattle; D002976:Clenbuterol / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D015394:Molecular Structure; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013113:Spin Labels; D013438:Sulfhydryl Compounds / Q000737:chemistry*
D013113:Spin Labels; D013438:Sulfhydryl Compounds; D012710:Serum Albumin, Bovine; D002976:Clenbuterol