Noninvolvement of surface lysine residues of bovine serum albumin in bilirubin binding.
Interaction of bilirubin with bovine serum albumin and its five succinylated forms was studied using fluorescence spectroscopy at two different ionic strengths i.e., 0.15 and 1.0 respectively. Affinity constant was found to be 1.8 x 10(7) litres/mole at 0.15 ionic strength which decreased to 4.4 x 10(6) litres/mole after 87% succinylation. On increasing ionic strength to 1.0, there was a slight decrease in affinity constant for native albumin. However, affinity constant remained same in 55 and 87% modified albumins at high ionic strength. These results suggest noninvolvement of surface lysine residues in bilirubin albumin complex.
Tayyab
S
S
Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, India.
Qasim
M A
MA
D001663:Bilirubin / Q000097:blood*; D008239:Lysine / Q000097:blood*; D011485:Protein Binding; D011487:Protein Conformation; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013387:Succinic Anhydrides; D013499:Surface Properties
D013387:Succinic Anhydrides; D012710:Serum Albumin, Bovine; C031801:succinic anhydride; D008239:Lysine; D001663:Bilirubin