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The sequence Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX.
Lenting PJ, van de Loo JW, Donath MJ, van Mourik JA, Mertens K. Lenting PJ, et al. Among authors: mertens k. J Biol Chem. 1996 Jan 26;271(4):1935-40. doi: 10.1074/jbc.271.4.1935. J Biol Chem. 1996. PMID: 8567641 Free article.
In previous studies have shown that the interaction between factor IXa and VIII involves the light chain of factor VIII and that this interaction inhibited by the monoclonal antibody CLB-CAg A against the factor VIII region Gln1778-Asp1840 (Lenting, P.J., Donath, M.J.S.H., van Mo …
In previous studies have shown that the interaction between factor IXa and VIII involves the light chain of factor VIII and that this intera …
Blood coagulation factor IX residues Glu78 and Arg94 provide a link between both epidermal growth factor-like domains that is crucial in the interaction with factor VIII light chain.
Christophe OD, Lenting PJ, Kolkman JA, Brownlee GG, Mertens K. Christophe OD, et al. Among authors: mertens k. J Biol Chem. 1998 Jan 2;273(1):222-7. doi: 10.1074/jbc.273.1.222. J Biol Chem. 1998. PMID: 9417068 Free article.
J., Christophe, O. D., ter Maat, H., Rees, D. J. G., and Mertens, K. (1996) J. Biol. Chem. 271, 25332-25337). In the present study, we have investigated the functional role of residue Glu78, which is not involved in calcium binding. ...Because Glu78 is conserved in …
J., Christophe, O. D., ter Maat, H., Rees, D. J. G., and Mertens, K. (1996) J. Biol. Chem. 271, 25332-25337). In the present s …
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