Antihemophilic factor was chromatographed on a homologous series of diaminoalkane-
and aminoalkane-modified Sepharose beads. Both factor VIII procoagulant activity (VIII:C)
and protein are retarded on these columns when compared to their elution on a column
made of unmodified Sepharose. Longer chains bind VIII:C and protein more tightly than
shorter chains. No bound activity could be eluted with ethylene glycol. Increasing
ionic strength eluted VIII:C and protein from aminoalkane- as well as from alkane-Sepharose.
It seems likely that hydrophobic, rather than ionic forces, are responsible for the
binding of VIII:C to the latter carriers.
Key words
Factor VIII - von Willebrand factor - Modified Sepharose - (Hydrophobic interaction)
chromatography
