Results 231 to 240 of about 641,383 (265)
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Bovine Serum Albumin Adsorption on Gluteraldehyde Cross-Linked Chitosan Hydrogels

, 2015
Chitosan hydrogels were cross-linked with glutaraldehyde and examined for the adsorption of a model protein (bovine serum albumin, BSA) at different pH and cross-linking ratios.
S. Mondal, Cunben Li, Kean Wang
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 ...
openaire   +3 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

Alteration of the Binding Strength of Dronedarone with Bovine Serum Albumin by β-Cyclodextrin: A Spectroscopic Study

, 2015
We report the influence of β-cyclodextrin on the binding of the drug dronedarone with bovine serum albumin. The stoichiometry, the binding constant, and the mode of binding of the derivative with β-cyclodextrin are studied by UV–Visible absorption ...
N. Sudha   +4 more
semanticscholar   +1 more source

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

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
openaire   +5 more sources

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.
openaire   +3 more sources

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 binding of penicillins to bovine serum albumin

Biochemical Pharmacology, 1966
Abstract The binding of phenoxymethylpenicillin and benzylpenicillin to bovine serum albumin has been studied over the pH range 1·5–10·0 in a variety of buffers. There was a marked reduction in binding above pH 9. The buffers used interfered with binding in the order trismaleate > veronal = chloride > phosphate.
openaire   +3 more sources

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