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Interaction of wogonin with bovine serum albumin

Bioorganic & Medicinal Chemistry, 2005
The binding of wogonin with bovine serum albumin (BSA) was investigated at different temperatures by fluorescence, circular dichroism (CD) and Fourier transform infrared spectroscopy (FT-IR) at pH7.40. The association constants K were determined by Stern-Volmer equation based on the quenching of the fluorescence of BSA in the presence of wogonin, which
Jiaqin Liu   +3 more
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The binding of atropine to bovine serum albumin

Biochemical Pharmacology, 1962
Abstract The binding of atropine to bovine serum albumin (BSA) as a model system was studied by ultrafiltration, spectrophotometry, and biological assay. Binding of atropine increased with an increase in pH from 5 to 8; the number of binding sites was approximately 20 at pH 6 and 100 at pH 8. Exhaustively acetylated BSA still bound some atropine when
Stephen I. Oroszlan   +1 more
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Trapping of by bovine serum albumin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974
Abstract When benzo (a) pyrene is shaken with bovine serum albumin solution, only a very small hydrocarbon fraction is bound to the protein (0.063 mole/mole). In contrast to this direct method, it is possible to trap more than 10 hydrocarbon molecules per albumin molecule by using a binary transient solvent, such as 2-chloroethanol-water. The
P. Bothorel, J.P. Desmazes
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Delayed Type Hypersensitivity to Bovine Serum Albumin and to Lipid-Conjugated Bovine Serum Albumin in Mice

International Archives of Allergy and Immunology, 1979
Delayed type hypersensitivity (DTH) to bovine serum albumin (BSA) and to lipid-conjugated BSA were studied comparatively. Unlike the case of BSA with which no DTH can be detected with native antigen, injection of butyric-conjugated BSA (Bu-BSA) in sensitized mice provokes a typical DTH for an early and limited period.
G Drach, J Chen-Marotel
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A method for the deionization of bovine serum albumin

Tissue Culture Association Manual, 1975
Bovine serum albumin has been used widely as a supportive medium for density gradient centrifugation (1) and (2) and as an essential component of culture medium for support of erythroid differentiation (3). Unfortunately most commercial lots of bovine serum albumin contain inhibitors which destroy the cells of interest.
Barker, J E, Nienhuis, A W
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Cationic bovine serum albumin based self-assembled nanoparticles as siRNA delivery vector for treating lung metastatic cancer.

Small, 2014
It is generally believed that intravenous application of cationic vectors is limited by the binding of abundant negatively charged serum components, which may cause rapid clearance of the therapeutic agent from the blood stream. However, previous studies
Jianfeng Han   +4 more
semanticscholar   +1 more source

Interaction of ochratoxin A with bovine serum albumin

Archives of Biochemistry and Biophysics, 1971
Abstract The interaction of ochratoxin A (OA) with bovine serum albumin (BSA) has been demonstrated by spectrophotometric, spectrophotofluorometric, equilibrium dialysis, and Sephadex gel filtration analyses. Spectrophotometric analysis revealed that the absorption maximum of OA shifts to a longer wavelength (near 395–400 nm) as a result of ...
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Thermal aggregation of glycated bovine serum albumin

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2010
Aggregation and glycation processes in proteins have a particular interest in medicine fields and in food technology. Serum albumins are model proteins which are able to self-assembly in aggregates and also sensitive to a non-enzymatic glycation in cases of diabetes.
Rondeau, P   +5 more
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Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study.

Molecular Biosystems, 2014
Binding of ascorbic acid (water-soluble antioxidant) and α-tocopherol (lipid-soluble antioxidant) to bovine serum albumin (BSA) has been studied using isothermal titration calorimetry (ITC), in combination with fluorescence spectroscopy, UV-vis ...
Xiangrong Li   +3 more
semanticscholar   +1 more source

THE ACYLATION OF BOVINE SERUM ALBUMIN WITH DIACETYLCYCLOSERINE

International Journal of Peptide and Protein Research, 1977
The reaction of the amino groups of bovine serum albumin (BSA) with diacetyl‐cycloserine (I) at pH 7.2–9.0 proceeded with both acylation by the diacetyl‐β‐aminooxy‐D‐alanyl (DAA) group and acetylation. The number of DAA groups was determined by their conversion to cycloserine (III) which can be accurately measured in micromolar amounts.
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