When albumin is prepared from human blood plasma by the cold ethanol method,
nonesterified long chain fatty acids present in the plasma do not strictly copurify with albumin.
About half of them are lost to the various globulin fractions precipitated in the first steps of
the fractionation procedure. A different behavior is observed for the short chain fatty acid,
caprylic acid. On the other hand, if fractionation of plasma proteins is done by ammonium
sulfate precipitation, both long and short chain fatty acids remain with the albumin.
Fibronectin was isolated from human blood plasma by affinity chromatography
on immobilized Physiogel, a plasma expander made by chemical degradation of gelatin.
Binding of fibronectin to Physiogel is weaker than to gelatin; elution could therefore be
performed under rather mild conditions: at pH 6.5 and 30°C. Loading of the sample at low
temperature increases the capacity of the affinity column.
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