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. 1985 May;82(9):2847–2851. doi: 10.1073/pnas.82.9.2847

Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX.

R A McGraw, L M Davis, C M Noyes, R L Lundblad, H R Roberts, J B Graham, D W Stafford
PMCID: PMC397663  PMID: 3857619

Abstract

We have independently isolated and characterized cDNA and genomic clones for the human coagulation factor IX. Sequence analysis in both cases indicates that threonine is encoded by the triplet ACT as the third residue of the activation peptide. This is in agreement with some earlier reports but in disagreement with others that show the alanine triplet GCT at this position. The discrepancy can thus be accounted for by natural variation of a single nucleotide in the normal population. Amino acid sequence analyses of activated factor IX from plasma samples of four individuals yielded two cases of alanine and two cases of threonine at the third position of the activation peptide. In factor IX from pooled plasma and in factor IX from a heterozygous individual, however, both alanine and threonine were found. Taken together, the findings show that a prevalent nondeleterious dimorphism exists in the activation peptide of human coagulation factor IX.

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Selected References

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