Fatty acid and drug binding to a low-affinity component of human serum albumin, purified by affinity chromatography.

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Vorum H, Pedersen AO, Honore B

Fatty acid and drug binding to a low-affinity component of human serum albumin, purified by affinity chromatography.

Int J Pept Protein Res. 1992 Nov;40(5):415-22.

PubMed ID

1483836 [ View in PubMed

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Abstract

Binding equilibria for decanoate to a defatted, commercially available human serum albumin preparation were investigated by dialysis exchange rate determinations. The binding isotherm could not be fitted by the general binding equation. It was necessary to assume that the preparation was a mixture of two albumin components about 40% of the albumin having high affinity and about 60% having low affinity. By affinity chromatography we succeeded in purifying the low-affinity component from the mixture. The high-affinity component, however, could not be isolated. We further analyzed the fatty acid and drug binding abilities of the low-affinity component. The fatty acids decanoate, laurate, myristate and palmitate were bound with higher affinity to the mixture than to the low-affinity component. Diazepam was bound with nearly the same affinity to the low-affinity component as to the albumin mixture, whereas warfarin was not bound at all to the low-affinity component.

DrugBank Data that Cites this Article

Drug Carriers

Drug	Carrier	Kind	Organism	Pharmacological Action	Actions
Capric acid	Serum albumin	Protein	Humans	No	Not Available	Details