Results 261 to 270 of about 717,908 (311)

Deuteron inactivation of dry bovine serum albumin

Archives of Biochemistry and Biophysics, 1954
Abstract The inactivation with deuterons of bovine serum albumin, as assayed by its ability to combine specifically with its homologous rabbit antiserum, is logarithmic when the samples are dissolved in phosphate buffer, indicating that the passage through the molecule of a single deuteron is capable of inactivating it.
W P, McNULTY, F, HUTCHINSON
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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
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Intrinsic viscosity of bovine serum albumin conformers

International Journal of Biological Macromolecules, 2008
Intrinsic viscosity of bovine serum albumin (BSA) at different pH values (2.7, 4.3, 7.4, 8 and 10) has been determined, as well as the Mark-Houwink constant and expansion factor. The traditional technique for data analysis using extrapolation to obtain intrinsic viscosity values shows an unusual behavior regarding concentration that can be observed in ...
Rolando, Curvale, Martin, Masuelli, Antonio Perez, Padilla   +2 more
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Mesostructure of fibrillar bovine serum albumin gels

International Journal of Biological Macromolecules, 2003
The mesostructure of bovine serum albumin (BSA) at low pH was investigated. Rheological measurements were performed to determine the critical percolation concentration (c(p)). A decreasing c(p) with increasing ionic strength was found. Fibrils with a contour length of about 100-300 nm were found using transmission electron microscopy.
Veerman, C., Heck, J., Sagis, L.M.C., van der Linden, E.   +3 more
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Prolidase contamination in commercial bovine serum albumin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1982
Bovine serum albumin from a number of commercial sources were screened for the presence or absence of peptidase contamination. Peptidase activity was monitored using various peptides as substrates. Two commercial preparations were found to have peptidase activity, and the enzyme was identified, on the basis of its substrate specificity, as prolidase ...
V, Ganapathy, M, Fonteles, D H, Pashley, F H, Leibach   +3 more
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Conjugate of bovine serum albumin with nicotine

Biochemical and Biophysical Research Communications, 1974
Abstract The preparation and characterization of a nicotine-albumin conjugate are reported. The nicotine derivative, 6-(p-aminobenzamido)nicotine, which was coupled to bovine serum albumin(BSA), was synthesized by the following sequence; 1 -nicotine→6-aminonicotine→6-(p-nitrobenzamido)nicotine→6-(p-aminobenzamido)nicotine.
H, Matsushita, M, Noguchi, E, Tamaki
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Adsorption of bovine serum albumin onto hydroxyapatite

Biomaterials, 1995
The adsorption of bovine serum albumin (BSA) onto hydroxyapatite (HA) has been studied as a function of protein concentration, pH and ionic strength. Isotherm data (adsorption being a reversible process) have been analysed using the Langmuir model, the adsorption parameters AT (maximum amount of protein adsorbed, mg m-2) and K (affinity constant, L g-1)
D T, Wassell, R C, Hall, G, Embery
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Ultrasonic spectroscopy in bovine serum albumin solutions

The Journal of the Acoustical Society of America, 1988
Ultrasonic absorption and velocity spectra in bovine serum albumin (BSA) aqueous solutions have been measured at 20 °C over the broad frequency range 0.1–1600 MHz in the pH range 1.5–13.2. Five different techniques were used: the plano–concave resonator, plano–plano resonator, pulse–echo overlap, Bragg reflection, and high-resolution Bragg reflection ...
P K, Choi, J R, Bae, K, Takagi
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Physicochemical studies of dinitrophenylated bovine serum albumin

International Journal of Peptide and Protein Research, 1982
The structural changes of bovine serum albumin (BSA) as a function of dini‐trophenylation have been studied by disc gel electrophoresis, sedimentation velocity analyses, and circular dichroism. These experiments were designed to understand the molecular bases for the change in immunogenicity and antigenicity of BSA upon dinitrophenylation ...
K F, Kessler, R F, Barth, K P, Wong
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Modified bovine serum albumin. II. Immunochemical studies

Archives of Biochemistry and Biophysics, 1957
Abstract Quantitative immunochemical studies were made of the homologous and heterologous reactions of bovine serum albumin; its deaminated, acetylated, and guanidinated derivatives; and the heat-treated products of these derivatives. It has been shown that the —NH 3 + groups per se do not participate in the interaction of BSA with its antibody ...
P H, MAURER, J, SRI RAM, S, EHRENPREIS
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