Abstract
Rabbit blood coagulation Factor XI was purified in 30% yield from plasma by ion exchange chromatography. The purified Factor XI zymogen gave a single protein band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence and absence of β-mercaptoethanol with an apparent molecular weight of 83,000. On alkaline disc gel electrophoresis Factor XI appeared either as a monomer or a dimer depending upon the conditions prior to electrophoresis. After dialysis against buffer at physiological pH and ionic strength Factor XI appeared as a monomer only. The apparent molecular weight of rabbit Factor XI in rabbit plasma on Sephadex G-200 chromatography was 200,000, probably reflecting a complex formed between high MW kininogen and Factor XI. The concentration of Factor XI in citrated normal rabbit plasma was 3.3 μg/ml.
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