Abstract
A 39 residue peptide from the tryptic digestion of bovine blood clotting factor X has been isolated by specific adsorption on barium citrate. The amino and carboxyl terminal sequences of the peptide were determined and compared to the vitamin K dependent Ca2+ binding region from bovine prothrombin. The factor X peptide was found to contain γ carboxyglutamic acid residues, and the results of independent analysis are consistent with all 14 glutamic acid residues as γ carboxyglutamic acid. The similarity of the factor X peptide to the prothrombin peptide supports the hypothesis that the vitamin K dependent blood clotting proteins are descended from a common ancestral gene.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1281-1285 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 72 |
| Issue number | 4 |
| DOIs | |
| State | Published - 1975 |