Results 311 to 320 of about 731,960 (357)
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Mesostructure of fibrillar bovine serum albumin gels
International Journal of Biological Macromolecules, 2003The 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. +3 more
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Prolidase contamination in commercial bovine serum albumin
Biochimica et Biophysica Acta (BBA) - General Subjects, 1982Bovine 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 +3 more
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Conjugate of bovine serum albumin with nicotine
Biochemical and Biophysical Research Communications, 1974Abstract 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, 1995The 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, 1988Ultrasonic 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, 1982The 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, 1957Abstract 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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Bovine serum albumin interacts with bacterial luciferase
Journal of Bioluminescence and Chemiluminescence, 1991AbstractBovine serum albumin (BSA) affects the amount of light obtained from bacterial luciferase by competing with luciferase for one of the luciferase substrates, the aldehyde. At low aldehyde concentrations BSA behaves as an inhibitor, but at high aldehyde concentrations BSA relieves substrate inhibition.
J C, Makemson, J W, Hastings
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Adsorption of bovine serum albumin on glass
Biochimica et Biophysica Acta, 1956Abstract 1. 1. The adsorption of bovine serum albumin on powdered pyrex glass has been studied as a function of protein concentration and of pH at an ionic strength of 0.05 and at 30°C. 2. 2. The surface area of the pyrex glass powder has been calibrated with the use of microscopic spherical glass particles. 3. 3. The limiting area of the
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Vitamin C-bovine serum albumin binding behaviour.
The Italian journal of biochemistry, 1987The binding of ascorbic acid and dehydroascorbic acid to bovine serum albumin is greatly heterogeneous. The Hill plots, as evaluated from the fluorescence quenching measurements, clearly show a biphasic behaviour. Scatchard analysis moreover indicates that the potency and the pattern of the binding can change gradually in the process of occupation of ...
Meucci, Elisabetta +5 more
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