UDP-Glucuronic Acid Binds First and the Aglycone Substrate Binds Second to Form a Ternary Complex in UGT1A9-Catalyzed Reactions, in Both the Presence and Absence of Bovine Serum Albumin

2012 ◽  
Vol 40 (11) ◽  
pp. 2192-2203 ◽  
Author(s):  
Nenad Manevski ◽  
Jari Yli-Kauhaluoma ◽  
Moshe Finel
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ternary Complex ◽  
Glucuronic Acid ◽  
Presence And Absence ◽  
Catalyzed Reactions

Interactions of cannabinoids with bovine serum albumin

1984 ◽  
Vol 4 (3) ◽  
pp. 239-243 ◽  
Author(s):  
S. J. Haque ◽  
M. K. Poddar
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Intensity ◽  
Binding Sites ◽  
Bovine Serum ◽  
Sulphonic Acid ◽  
Ans Binding ◽  
Emission Maximum ◽  
Quenching Of Fluorescence ◽  
Presence And Absence

There is no shift of emission maximum (F470nm) of bovine serum albumin (BSA)-l-anilino-8-naphthatene sulphonic acid (ANS) complex in the pesence of delta-9-tetrahydrocannabinol (delta-9-THC) alone and cannabidiol (CBD) or cannabinol (CBN) in the presence and absence of delta-9-THC. Delta-9-THC (1.66–13.33 μM) and CBD at higher concentrations (13.33–20.0 μM) produce a concentration-dependent significant quenching of fluorescence of BSA-ANS complex, but CBN (l.66–20.0 μM) as well as CBD at lower concentrations (1.66–6.66 μM) fails to produce any significant change in Iluorescence intensity under similar conditions. Furthermore, neither CBD nor CBN is able to affect the delta-9-THC-induced quenching of fluorescence intensity of BSA-ANS complex. These results indicate that the binding of cannabinoids to the ANS binding sites of BSA molecule are in the order detta-9-THC > CBr3 > CBN, and CBD or CBN does not have any influence on the binding of delta-9-THC to BSA molecules under these conditions.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

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