Results 301 to 310 of about 877,460 (349)
Some of the next articles are maybe not open access.
Ionization of Bovine Serum Albumin Monolayers
Nature, 1952IT has long been known that the surface electrical potential of a protein monolayer at the air/water interface is dependent on the pH and the nature of the ions present in the aqueous sub-solution. There is no record, however, of a comprehensive investigation of the variation of protein surface potential with the pH of the sub-solution.
M. Z. Dogan, J. Glazer
openaire +3 more sources
Binding of isofraxidin to bovine serum albumin
Biopolymers, 2004AbstractThe binding of isofraxidin to bovine serum albumin (BSA) was studied under physiological conditions with BSA concentration of 1.5×10−6 mol · L−1 and drug concentration in the range of 1.67×10−6 mol · L−1 to 2.0×10−5 mol · L−1. Fluorescence quenching spectra in combination with uv absorption spectroscopy, Fourier transform infrared (FTIR ...
Jiaqin Liu +3 more
openaire +3 more sources
Immunochemistry of Bovine Serum Albumin
1978Two fragments were isolated from BSA one was derived from the first terminal third of the molecule and the second from the last third of the molecule. Each fragment inhibited the reaction of BSA-anti BSA by 90% or better. An immunoabsorbent of each bound 90% of anti BSA. Each fragment bound two antibody molecules per mole of fragment. These results are
openaire +3 more sources
Elucidating the interaction of limonene with bovine serum albumin: a multi-technique approach.
Molecular Biosystems, 2015The interaction of Bovine Serum Albumin (BSA) with limonene has been studied by UV-visible spectroscopy, fluorescence spectroscopy and molecular docking, and its effects on protein conformation, topology and stability were determined by Circular ...
S. Chaturvedi +5 more
semanticscholar +1 more source
Interaction of acrylamide with bovine serum albumin
Environmental Research, 1986The binding of acrylamide (ACR) with purified bovine serum albumin (BSA) was studied. Binding of ACR with BSA was characterized by equilibrium dialysis, fluorescence studies, and ultraviolet spectroscopy. ACR was quantitated by high-pressure liquid chromatography.
Prahlad K. Seth +3 more
openaire +3 more sources
Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin.
Journal of Physical Chemistry B, 2015Disulfide bonds are naturally formed in more than 50% of amyloidogenic proteins, but the exact role of disulfide bonds in protein aggregation is still not well-understood.
Mu Yang, Colina Dutta, A. Tiwari
semanticscholar +1 more source
Adsorption of bovine serum albumin on glass
Biochimica et Biophysica Acta, 1956Abstract 1. 1. The adsorption of bovine serum albumin on powdered pyrex glass has been studied as a function of protein concentration and of pH at an ionic strength of 0.05 and at 30°C. 2. 2. The surface area of the pyrex glass powder has been calibrated with the use of microscopic spherical glass particles. 3. 3. The limiting area of the
openaire +3 more sources
Binding of noradrenaline to bovine serum albumin
International Journal of Nuclear Medicine and Biology, 1981Abstract The binding of noradrenaline to bovine serum albumin (40 mg ml −1 ) has been studied by gel filtration. Over the range of 5 × 10 −9 M to 10 −3 M of noradrenaline, the data obtained fit a model with three classes of noninteracting binding sites: a high affinity-low capacity site with a K A of 1.18 × 10 6 M −1 and a capacity of 11.84 ...
Y. Cohen, E. Rodriguez Farre
openaire +3 more sources
Complexes of Dendrimers with Bovine Serum Albumin
Biomacromolecules, 2010We report the complexation of bovine serum albumin (BSA) with several dendrimers of different compositions mPEG-PAMAM (G3), mPEG-PAMAM (G4), and PAMAM (G4) at physiological conditions using constant protein concentration and various dendrimer contents.
J. S. Mandeville +1 more
openaire +2 more sources
The interaction of rivanol with bovine serum albumin
Archives of Biochemistry and Biophysics, 1961Abstract Interaction of the cationic form of rivanol (6, 9-diamino-2-ethoxyacridine lactate) with native and modified bovine serum albumins (BSA) was studied by various physicochemical methods. Influence of pH and ionic strength on precipitation of BSA by rivanol was investigated.
Abraham Saifer +2 more
openaire +3 more sources