Results 271 to 280 of about 960,873 (349)
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The cryoaggregation of bovine serum albumin

Cryobiology, 1970
Summary Bovine serum albumin in the native (BSA), reduced (BSA-SH), and combined (BSA-S-NEM) forms was frozen at −5°C. The BSA remained essentially soluble; the BSA-SH and BSA-S-NEM both aggregated nearly completely when allowed to reimbibe water at room temperature but to a smaller degree when allowed to reimbibe just above the freezing point.
R, Goodin, J, Levitt
openaire   +2 more sources

Effect of heating and ionic strength on the interaction of bovine serum albumin and the antinutrients tannic and phytic acids, and its influence on in vitro protein digestibility.

Food Chemistry, 2018
Bioavailability of food nutrients can be reduced in the presence of antinutrients such as phytates and tannins. This work aimed to study bovine serum albumin binding to phytic acid and tannic acid, and its influence on in vitro protein digestibility. The
Elaine Kaspchak   +2 more
semanticscholar   +1 more source

Applications of human and bovine serum albumins in biomedical engineering: A review.

International Journal of Biological Macromolecules, 2023
Serum albumin, commonly recognized as a predominant major plasma protein, is ubiquitously distributed among vertebrates, demonstrating versatility and widespread accessibility.
Xinhao Xu   +7 more
semanticscholar   +1 more source

Raman studies of bovine serum albumin

Biopolymers, 1976
AbstractThe Raman Spectra of bovine serum albumin have been obtained in the solute state, in alkaline and acidic solutions, and in the gel. The reversible denaturations of bovine serum albumin solutions by heat, acid's, and alkali were studied and a new mechanism for heat denaturation has been proposed based on a continuous unfolding of the α‐helices.
V J, Lin, J L, Koenig
openaire   +2 more sources

Ionization of Bovine Serum Albumin Monolayers

Nature, 1952
IT 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   +2 more sources

Food anaphylaxis to bovine serum albumin

Journal of Allergy and Clinical Immunology, 1998
Although rare, anaphylaxis has been reported after topical administration of bacitracin ointment.1-7 All reported patients, including ours, had applied the drug to a compromised skin barrier (i.e., leg ulcers, excoriated dermatitis, or burns). Thus ready access to the systemic circulation seems to be a prerequisite for the development of anaphylaxis ...
G, Kanny   +2 more
openaire   +2 more sources

Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12

Spectroscopy Letters, 2018
The conformation of bovine serum albumin largely depends on its microenvironment pH and affects its physical functions and applications. In this study, we investigated the effects of pH (wide range 2–12) on the conformation of bovine serum albumin based ...
Zhenxing Chi   +5 more
semanticscholar   +1 more source

Antioxidant benzimidazole bind bovine serum albumin

Journal of Photochemistry and Photobiology B: Biology, 2012
1-(4-Methoxybenzyl)-2-(4-methoxyphenyl)-1H-benzo[d]imidazole (MBMPB) was synthesized and characterized by (1)H NMR, (13)C NMR, Mass and IR spectral analysis. The mutual interaction of MBMPB with bovine serum albumin (BSA) was investigated using solution spectral studies.
J, Jayabharathi   +2 more
openaire   +2 more sources

Immunogenicity of Insolubilized Bovine Serum Albumin

The Journal of Immunology, 1966
Summary As compared with soluble bovine serum albumin, the use of the heat-denatured protein as an immunizing antigen in rabbits resulted both in a larger number of responding animals and in markedly higher serum antibody titers. In measuring these titers, it was found that the lower the serum titer, the higher was the ...
A A, Hirata, D H, Sussdorf
openaire   +2 more sources

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   +3 more sources

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