Results 251 to 260 of about 492,888 (308)

Antigenic Determinants of Bovine Serum Albumin

International Archives of Allergy and Immunology, 2001
<i>Background:</i> Bovine serum albumin (BSA) is one of the most widely studied proteins; its structure is well known and its antigenic characteristics have been described in several papers. The aim of this research was the identification of the BSA antigenic determinants.
Beretta B, Conti A, Fiocchi A, Gaiaschi A, Galli, C L, Giuffrida, M G, Ballabio C, Restani, P   +10 more
openaire   +3 more sources

THE COMBINATION OF HEPARIN AND BOVINE SERUM ALBUMIN

Canadian Journal of Medical Sciences, 1953
The complexing of heparin and bovine serum albumin in acetate buffer at pH 5.0 was studied by electrophoretic techniques. A stable complex with a heparin : albumin mole ratio of 1 : 2 was found, though there was evidence for the existence of unstable complexes with a higher heparin : albumin ratio.
D W, CLARKE, F C, MONKHOUSE
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Factors Affecting the Synthesis of Bovine Serum Albumin Nanoparticles Using the Desolvation Method

Nanotechnology, Science and Applications
Yenni Puspita Tanjung,1,2 Mayang Kusuma Dewi,1 Vesara Ardhe Gatera,3,4 Melisa Intan Barliana,3,5 I Made Joni,6,7 Anis Yohana Chaerunisaa1 1Department of Pharmaceutics and Pharmaceutical Technology, Faculty of Pharmacy, Universitas Padjadjaran, Bandung ...
Mayang Kusuma Dewi, Vesara Ardhe Gatera, Melisa Intan Barliana   +2 more
exaly   +1 more source

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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

Aggregation and fibrillation of bovine serum albumin

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007
The all-alpha helix multi-domain protein bovine serum albumin (BSA) aggregates at elevated temperatures. Here we show that these thermal aggregates have amyloid properties. They bind the fibril-specific dyes Thioflavin T and Congo Red, show elongated although somewhat worm-like morphology and characteristic amyloid X-ray fiber diffraction peaks ...
Holm, NK, Jespersen, SK, Thomassen, LV, Wolff, TY, Sehgal, P, Thomsen, LA, Christiansen, Gunna, Andersen, CB, Knudsen, AD, Otzen, DE   +9 more
openaire   +4 more sources

The heterogeneity of bovine serum albumin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1966
Abstract 1. 1. The different components of native and modified bovine serum albumin have been investigated with respect to differences in composition and structure. It was found that native bovine serum albumin is composed of at least 3 components, and that most bovine serum albumin samples contain 4.
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Binding of isofraxidin to bovine serum albumin

Biopolymers, 2004
AbstractThe 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, Jianniao, Tian, Zhide, Hu, Xingguo, Chen   +3 more
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Binding of noradrenaline to bovine serum albumin

International Journal of Nuclear Medicine and Biology, 1981
Abstract 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 ...
E R, Farre, Y, Cohen
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Complexes of Dendrimers with Bovine Serum Albumin

Biomacromolecules, 2010
We 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, H A, Tajmir-Riahi
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