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Gene Review

F2  -  coagulation factor II (thrombin)

Bos taurus

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High impact information on F2

  • The synthesis of the amino acid sequence found in bovine prothrombin precursor 13-29 (PTP 13-29) has been achieved by solid-phase synthesis of the bis(acetamidomethyl)-protected linear peptide followed by cyclization to the monomeric disulfide [1].
  • Plasma abnormal prothrombin and microsomal prothrombin precursor in various species (38492) [2].
  • CONCLUSIONS: The F2 kringle domain in mzTBN-F1 is bound to the electropositive heparin-binding site on thrombin in an orientation that is systematically shifted and has significantly more interdomain contacts compared to a noncovalent complex of free F2 and free thrombin [3].
  • Analysis of F2 subunits in their deglycosylated forms indicated that the difference in the molecular weights of the F2 subunits was due to the difference in the extent of glycosylation [4].
  • To delineate the molecular basis for differences in the molecular weights of F2 subunits among the BRSV strains, the nucleotide sequences of the F genes of FS1 and VC464 strains were determined from cDNA clones [4].

Anatomical context of F2

  • The vitamin K-dependent carboxylase activity of bovine liver microsomes has been purified 500-fold by adsorption to an antiprothrombin column and elution with a dodeca peptide which competes with a prothrombin precursor enzyme recognition site [5].

Analytical, diagnostic and therapeutic context of F2


  1. Synthetic bovine prothrombin precursor 13-29 for studies of vitamin K dependent carboxylase. Pottorf, R.S., Rich, D.H., Engelke, J., Suttie, J.W. J. Med. Chem. (1987) [Pubmed]
  2. Plasma abnormal prothrombin and microsomal prothrombin precursor in various species (38492). Carlisle, T.L., Shah, D.V., Schlegel, R., Suttie, J.W. Proc. Soc. Exp. Biol. Med. (1975) [Pubmed]
  3. New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK. Martin, P.D., Malkowski, M.G., Box, J., Esmon, C.T., Edwards, B.F. Structure (1997) [Pubmed]
  4. Structure and sequence comparison of bovine respiratory syncytial virus fusion protein. Pastey, M.K., Samal, S.K. Virus Res. (1993) [Pubmed]
  5. Vitamin K-dependent carboxylase: partial purification of the enzyme by antibody affinity techniques. Harbeck, M.C., Cheung, A.Y., Suttie, J.W. Thromb. Res. (1989) [Pubmed]
  6. Purification and identification of bovine liver gamma-carboxylase. Berkner, K.L., Harbeck, M., Lingenfelter, S., Bailey, C., Sanders-Hinck, C.M., Suttie, J.W. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
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