Interaction of alpinetin with bovine serum albumin: Probing of the mechanism and binding site by spectroscopic methods

2010 ◽  
Vol 76 (3-4) ◽  
pp. 410-417 ◽  
Author(s):  
Guowen Zhang ◽  
Nan Zhao ◽  
Xing Hu ◽  
Jiao Tian
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Spectroscopic Methods

scholarly journals Interactions of rat α-foetoprotein with bilirubin

1979 ◽  
Vol 179 (3) ◽  
pp. 705-707 ◽  
Author(s):  
V Versée ◽  
A O Barel
Keyword(s):  
Absorption Spectrum ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Oxidation Rate ◽  
Bovine Serum ◽  
Bile Pigment ◽  
Binding Parameters ◽  
Enzymic Oxidation ◽  
Bilirubin Binding

The binding of bilirubin to rat-alpha-foetoprotein has been measured by changes in the absorption spectrum and by the appearance of two intense circular-dichroism bands. Furthermore binding of this bile pigment has been demonstrated by a decrease of its enzymic oxidation rate and by competition experiments with bovine serum albumin-agarose. The binding parameters have been determined as follows: n = 1.0 mol bound/mol of protein and Ka = 2.9 × 10(6) M-1. Competition of oestradiol for the bilirubin-binding site has not been established.

A study of the interaction between bromopyrogallol red and bovine serum albumin by spectroscopic methods

2007 ◽  
Vol 73 (2) ◽  
pp. 211-216 ◽  
Author(s):  
S.M.T. Shaikh ◽  
J. Seetharamappa ◽  
S. Ashoka ◽  
P.B. Kandagal
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Methods ◽  
Bromopyrogallol Red
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