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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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Antigenicity of Chemically Modified Bovine Serum Albumin
The Journal of Immunology, 1967Summary Extensive modification of bovine serum albumin (BSA) by guanidination, nitroguanidination and amidination did not greatly affect the ability of modified BSA to precipitate with anti-BSA antibodies. The ability of succinylated BSA to precipitate with heterologous antibodies was influenced by the conformation of the antigen as ...
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