Publications by authors named "Richard G Hiskey"
An IgM monoclonal antibody, S11-23.4, raised against the 47-62 amino acid sequence in bovine prothrombin fragment 1 (F-1, the amino-terminal 156 residues of prothrombin), was purified from tissue culture supernatants and ascites using different purification schemes to determine the best method. There are many different purification schemes for the purification of IgG antibodies, which are generally easier to purify than IgM antibodies.
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- Bovine prothrombin fragment 1 (F-1) is examined for its ability to bind calcium ions (Ca(II)) and phospholipids, focusing on two key segments: 35-46 and 47-62.
- The 35-46 segment has an alpha-helix and aromatic residues crucial for phospholipid binding, while the 47-62 segment stabilizes the protein’s structure with a disulfide loop.
- Monoclonal antibodies were created against both regions, revealing that the antibody binding is influenced by the presence of metal ions, particularly Ca(II), which enhances the affinity for F-1.