The Malmo polymorphism of coagulation factor IX, an immunologic polymorphism due to dimorphism of residue 148 that is in linkage disequilibrium with two other F.IX polymorphisms

Graham, J. B.
Lubahn, D. B.
Lord, S. T.
Kirshtein, J.
Nilsson, Inga Marie
Wallmark, A.
Ljung, R.
Frazier, L. D.
Ware, J. L.
Wah Lin, S.
Stafford, D. W.
Bosco, J.

Publication date

January 1988

Publisher

Cell Press

Abstract

A mouse monoclonal antibody (MAB 9,9) to coagulation factor IX (F.IX) detects a polymorphism in the plasma of normal people. Its epitope has been narrowed down to <6 amino acids in the activation peptide of the X-linked F.IX protein. The activation peptide contains a dimorphism - Thr:Ala - at position 148 of the protein. Using synthetic oligonucleotides, we have demonstrated that (1) the F.IX which reacts with 9.9 has Thr at position 148 and (2) that which does not has Ala. Positive reactors (148(thr)) are designated Malmo A, and negative reactors (148(ala)) are designated Malmo B. The plasma levels of AA women are indistinguishable from those of A men, and both B men and BB women are null against MAB 9.9. The plasma level of Malmo A in AB ...

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The Malmo polymorphism of coagulation factor IX, an immunologic polymorphism due to dimorphism of residue 148 that is in linkage disequilibrium with two other F.IX polymorphisms

Abstract

Extracted data

The Malmo polymorphism of coagulation factor IX, an immunologic polymorphism due to dimorphism of residue 148 that is in linkage disequilibrium with two other F.IX polymorphisms

Abstract

Extracted data

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