Results 231 to 240 of about 1,184,647 (254)

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, NAVARRA, Giovanna, Cacciabaudo, F, LEONE, Maurizio, Bourdon, E, MILITELLO, Valeria   +5 more
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Interaction of ochratoxin A with bovine serum albumin

Archives of Biochemistry and Biophysics, 1971
Abstract The interaction of ochratoxin A (OA) with bovine serum albumin (BSA) has been demonstrated by spectrophotometric, spectrophotofluorometric, equilibrium dialysis, and Sephadex gel filtration analyses. Spectrophotometric analysis revealed that the absorption maximum of OA shifts to a longer wavelength (near 395–400 nm) as a result of ...
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THE ACYLATION OF BOVINE SERUM ALBUMIN WITH DIACETYLCYCLOSERINE

International Journal of Peptide and Protein Research, 1977
The reaction of the amino groups of bovine serum albumin (BSA) with diacetyl‐cycloserine (I) at pH 7.2–9.0 proceeded with both acylation by the diacetyl‐β‐aminooxy‐D‐alanyl (DAA) group and acetylation. The number of DAA groups was determined by their conversion to cycloserine (III) which can be accurately measured in micromolar amounts.
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The binding of penicillins to bovine serum albumin

Biochemical Pharmacology, 1966
Abstract The binding of phenoxymethylpenicillin and benzylpenicillin to bovine serum albumin has been studied over the pH range 1·5–10·0 in a variety of buffers. There was a marked reduction in binding above pH 9. The buffers used interfered with binding in the order trismaleate > veronal = chloride > phosphate.
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The binding of ascorbate to bovine serum albumin.

International journal for vitamin and nutrition research. Internationale Zeitschrift fur Vitamin- und Ernahrungsforschung. Journal international de vitaminologie et de nutrition, 1984
Ultrafiltration has been used to investigate the interaction of ascorbate with bovine serum albumin in 0.1 M sodium phosphate buffer, pH 6.5. The results are interpreted in terms of the binding of ascorbate to four equivalent and independent protein sites, governed by an intrinsic association constant of 2 600 +/- 700 M-1 at 20 degrees C, thereby ...
Oelrichs B.A., Kratzing C.C., Kelly J.D., Winzor D.J.   +3 more
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The binding of phenol red by serum and by bovine serum albumin

Archives of Biochemistry and Biophysics, 1961
Abstract Serum proteins from four species were shown to interact with the anions of phenol red. The extent of indicator-protein interaction, studied by a combination of spectrophotometry and ultrafiltration, was found to be highly species dependent.
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Binding of Salicylate to Crystalline Bovine Serum Albumin and to Fraction V Bovine Serum Albumin

Journal of Pharmaceutical Sciences, 1970
H B, Kostenbauder, S M, Bahal, M J, Jawad   +2 more
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Investigation of the interaction between acridine orange and bovine serum albumin

Talanta, 1998
Chunli Bai, Zhang Lin, Xi-Zeng Feng
exaly  

18β-Glycyrrhetinic acid interaction with bovine serum albumin

Journal of Photochemistry and Photobiology A: Chemistry, 2007
Yi-Zeng Liang
exaly  

Bovine serum albumin

2016
openaire   +1 more source