Journal ArticleDOI
A polarographic investigation of the binding properties of Serum Albumin
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It has been shown that the binding capacity of dissolved serum albumin for methyl orange increases on dilution, and the increased binding capacity implies a change in the protein molecule.Abstract:
It has been shown that the binding capacity of dissolved serum albumin for methyl orange increases on dilution. The increased binding capacity implies a change in the protein molecule. The possible nature of this change is discussed.read more
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Book ChapterDOI
Chapter 6 – Plasma Albumin
TL;DR: Two striking properties stand out upon examination of the literature on plasma albumin: the unusual affinity for ions, particularly anions, and the remarkable degree to which the molecule is capable of undergoing extensive conformational alterations apparently in a fully reversible manner.
Journal ArticleDOI
Steroid-protein interactions studied by fluorescence quenching
Nicola A. Attallah,Gene F. Lata +1 more
TL;DR: The results suggest that testosterone binding may alter bovine serum albumin conformation and that the measured binding capacity of this protein for testosterone is dependent on the protein concentration.
Journal ArticleDOI
Binding of phenytoin, L-tryptophan and O-methyl red to albumin. Unexpected effect of albumin concentration on the binding of phenytoin and L-tryptophan.
TL;DR: Values for the apparent association constant ( k ) and number of binding sites ( n ) could not be obtained from these plots, but it was apparent that n and/or k decrease as albumin concentration increases.
Journal ArticleDOI
A solid-phase optoelectronic sensor for serum albumin
M.J. Goldfinch,C.R. Lowe +1 more
TL;DR: A simple solid-phase optoelectronic sensor for serum albumin covalently attached to a cellophane membrane is sandwiched between a red light emitting diode and a silicon photodiode with integral amplifier.