Summary
The anti-hemophilic factor (AHF, factor VIII) has been separated from fibrinogen by
means of continous flow electrophoresis. The starting material was Cohn’s fraction
I, prepared from normal human resinplasma. These fibrinogen-free products still contained
proteins without AHF-activity. Part of these contaminating proteins could be extracted
from fraction I by means of a 1 molar solution of epsilon amino caproic acid. The
residue, principally consisting of fibrinogen and AHF, was dissolved in a triethylamine
buffer and subjected to continuous flow electrophoresis. The resulting AHF-preparations
were free from fibrinogen. By immuno-electrophoresis no proteins without AHF-activity
could be demonstrated in these preparations.