The interaction of rDNA factor VIII, factor VIIIdes-797-1562 and factor VIIIdes-797-1562-derived peptides with phospholipid.
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.
D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D005169:Factor VIII / Q000031:analogs & derivatives* / Q000378:metabolism; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism*; D010743:Phospholipids / Q000097:blood*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism
D010446:Peptide Fragments; D010743:Phospholipids; D011994:Recombinant Proteins; C055312:factor VIII (des-797-1562); D005169:Factor VIII