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.

scholarly journals In vitro Model for Studying Interactions between Ketorolac and Omeprazole with Bovine Serum Albumin by UV-Spectroscopic Method

2015 ◽  
Vol 17 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Kanij Nahar Deepa ◽  
Md Khalid Hossain ◽  
Md Shah Amran ◽  
Shaila Kabir
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Association Constant ◽  
Spectroscopic Method ◽  
Free Fraction ◽  
In Vivo Model ◽  
Specific Probe

The binding of Ketorolac and Omeprazole to bovine serum albumin (BSA) was studied by equilibrium dialysis method followed by UV spectroscopy. Warfarin and Diazepam were used as site-I and site-II specific probe, respectively. The binding of Ketorolac and Omeprazole was characterized by two sets of association constant: high affinity association constant (K1) with low capacity binding site (n1) and low affinity association constant (K1) with high capacity binding site (n1). In this study, n1 and n1 values were found to be 0.25 ± 0.006 and 1.8 ± 0.025 for Ketorolac and 0.22 ± 0.030 and 1.3±0.035 for Omeprazole at pH 7.4 and 37°C, respectively. At the same condition, the values of K1 and K1 for Ketorolac were found to be 0.624 ± 0.033 ?M-1 and 0.133 ± 0.023 ?M-1 and that of Omeprazole were 0.51 ± 0.001 ?M-1 and 0.28 ± 0.005 ?M-1, respectively. Site specific probe displacement studies implied that both Ketorolac and Omeprazole bind predominantly to site-II, the Diazepam site. In the present study, both Ketorolac and Omeprazole increased the free fraction of each other when they simultaneously bound to BSA. They compete for a common binding site on the albumin molecule, thereby free fraction of both the drugs was increased as compared to the level obtained when the drugs were given individually. We, thus, conclude that during concurrent administration of Ketorolac and Omeprazole adequate precautions should be taken. However, further studies are needed on in-vivo model to substantiate the findings from in-vitro experiments. DOI: http://dx.doi.org/10.3329/bpj.v17i1.22323 Bangladesh Pharmaceutical Journal 17(1): 92-98, 2014

scholarly journals Location of naphthol yellow-S binding site on bovine serum albumin.

1981 ◽  
Vol 4 (11) ◽  
pp. 851-859
Author(s):  
MOTOHARU IWATSURU ◽  
HIDEO NISHIGORI ◽  
KAZUO MARUYAMA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum

scholarly journals THE EFFECT OF LITHIUM PERIODATE ON CRYSTALLINE BOVINE SERUM ALBUMIN

1949 ◽  
Vol 89 (5) ◽  
pp. 479-489 ◽  
Author(s):  
Walther F. Goebel ◽  
Gertrude E. Perlmann
Keyword(s):  
Amino Acids ◽  
Absorption Spectrum ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Experimental Animals ◽  
Bovine Albumin ◽  
Electrophoretic Behavior ◽  
Prolonged Contact ◽  
Immunological Changes

A study of the chemical, physicochemical, and immunological changes in bovine serum albumin, brought about by oxidation with lithium periodate, has been made. It has been shown that destruction of certain amino acids occurs, that a change in the absorption spectrum takes place, and that the electrophoretic behavior of the protein is altered. Prolonged contact of bovine albumin with lithium periodate destroys its ability to incite antibodies in experimental animals.

scholarly journals Evidence in liver for a disulphide-linked scavenger receptor containing a binding site for acetylated low-density lipoprotein and maleylated bovine serum albumin

1988 ◽  
Vol 253 (3) ◽  
pp. 835-838 ◽  
Author(s):  
E Ottnad ◽  
D P Via ◽  
H Sinn ◽  
E Friedrich ◽  
R Ziegler ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Scavenger Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Bsa Binding ◽  
35 Kda Protein

Membranes from rat liver were analysed under reducing conditions. The components of the soluble membranes responsible for the binding of acetylated low density lipoprotein (acetyl-LDL) and maleylated bovine serum albumin (Mal-BSA) were chromatographed on a polyethyleneimine-cellulose column and subsequently separated by gel electrophoresis. For both ligands a major binding protein (Mr = 35,000) was revealed by ligand blotting. A minor protein (Mr greater than 67,000) exhibited little binding. The Scatchard plot of the 131I-Mal-BSA binding data of the 35 kDa protein was linear, with a Kd of 17.3 nM. High concentrations of acetyl-LDL competed for half of the 131I-Mal-BSA binding. Excessive Mal-BSA competed for all the visible acetyl-LDL binding. The findings indicate the existence, in the reduced hepatic membrane, of a 35 kDa protein that has two binding sites for 131I-Mal-BSA and one binding site for acetyl-LDL.

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