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Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes
Published on: June 3, 2014
The interaction of rDNA factor VIII, factor VIIIdes-797-1562 and factor VIIIdes-797-1562-derived peptides with
1Protein Purification Research, Cutter Biological Miles Laboratories, Berkeley, CA 94710.
Abstract:
The interaction of rDNA factor VIII, factor VIIIdes-797-1562 and factor VIIIdes-797-1562-derived peptides with phospholipid were studied with an ELISA system. Factor VIII was observed to bind to phosphatidylserine but not to phosphatidylcholine or phosphatidylethanolamine. Factor VIIIdes-797-1562 also bound to phosphatidylserine with the same affinity, suggesting that residues 797-1562 of the factor VIII molecule are not required for phospholipid binding. In addition, the binding of the purified factor VIII carboxy-terminal Mr 80,000 and amino-terminal Mr 90,000/115,000 polypeptides to phosphatidylserine was investigated. Only the Mr 80,000 polypeptide was observed to bind, suggesting that the carboxy-terminal of factor VIII contains the lipid binding domain.
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