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Characterization of an almost full-length cDNA coding for human blood coagulation factor X.
A human liver cDNA library was screened by colony hybridization with a bovine factor X cDNA probe. Three of the positive plasmids contained overlapping DNA that coded for most of human factor X mRNA. DNA sequence analysis of these three clones allowed the prediction of the complete amino acid sequence of plasma factor X. From these studies, we predict that human factor X is synthesized as a single polypeptide chain precursor in which the light and heavy chains of plasma factor X are linked by the tripeptide Arg-Lys-Arg. The cDNA sequence also predicts that human factor X is synthesized as a preproprotein having an amino-terminal leader peptide of at least 28 amino acid residues. A comparison of the amino acid sequences of human and bovine factor X shows high sequence identity around the calcium-binding regions and catalytic regions but low sequence identity around the nonfunctional regions.
PMID: 2582420 [PubMed - indexed for MEDLINE]
PMCID: PMC397831
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Cited by 21 PubMed Central articles
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Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G defines an alternative pathway of leucocyte initiation of coagulation.
Plescia J, Altieri DC.
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[Biochem J. 1996]
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Inhibition of leukocyte-endothelial cell interactions and inflammation by peptides from a bacterial adhesin which mimic coagulation factor X.
Rozdzinski E, Sandros J, van der Flier M, Young A, Spellerberg B, Bhattacharyya C, Straub J, Musso G, Putney S, Starzyk R.
J Clin Invest. 1995 Mar; 95(3):1078-85.
[J Clin Invest. 1995]
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Polymorphism associated with the human coagulation factor X (F10) gene.
Jaye M, Ricca G, Kaplan R, Howk R, Mudd R, Ngo KY, Fair DS, Drohan W.
Nucleic Acids Res. 1985 Nov 25; 13(22):8286.
[Nucleic Acids Res. 1985]
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