Results 301 to 310 of about 650,535 (339)
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Bovine Serum Albumin Adsorption on Gluteraldehyde Cross-Linked Chitosan Hydrogels
, 2015Chitosan 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
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Trapping of by bovine serum albumin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974Abstract 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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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
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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
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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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, 1975Bovine 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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Binding of ascorbic acid and α-tocopherol to bovine serum albumin: a comparative study.
Molecular Biosystems, 2014Binding 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
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Interaction of ochratoxin A with bovine serum albumin
Archives of Biochemistry and Biophysics, 1971Abstract 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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THE ACYLATION OF BOVINE SERUM ALBUMIN WITH DIACETYLCYCLOSERINE
International Journal of Peptide and Protein Research, 1977The 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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The binding of penicillins to bovine serum albumin
Biochemical Pharmacology, 1966Abstract 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.
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