Binding of the anti-inflammatory drug niflumic acid to bovine serum albumin

Binding of the anti-inflammatory drug niflumic acid to serum albumin was measured by equilibrium dialysis and the dissociation constants were determined. The maximal binding capacity was 36 mol niflumic acid per mol albumin. Most of the binding sites were of low affinity, only six having dissociation constants below 1 mM. At the plsma concentrations most frequently used in eperimental work, the high affinity sites account for more than 99% of the albumin-bound influmic acid

The influence of albumin on palmitate transport in the isolated perfused rat liver

Unidirectional fluxes (influx and efflux) and the net flux of palmitate across the hepatocyte membrane were measured in the intact rat liver employing the multiple indicator dilution technique. At albumin concentrations in the range between 0.1 and 0.5 mM the influx rate was 2.3 times greater than that of the net flux. The rate of efflux was somewhat higher than the net flux, indicating that palmitate undergoes an exchange process across the liver cell membranes with efflux to the extracellular albumin site being significant. At. lower albumin concentrations, hower, the influx/net flux approached unit, implying that transport becomes a rate-limiting factor for metabolism

Octanoate transport in the isolated, perfused rat liver

The multiple indicator dilution technique was used to investigate octanoate transport in the isolated, perfused rat liver. The form of the octanoate outflow profiles depends on albumin concentration. The steady-state intracellular octanoate concentration and the rate of uptake increase when the albumin concentration is decreased. At physiological albumin concentrations, the intracellular concentration of octanoate is only 7% of the extracellular concentration. Exchange between the intra-and extracellular space, however, is very rapid, irrespective of the albumin concentration and consequently exchange is not rate limiting for metabolism