Characterization of an almost full-length cDNA coding for human blood coagulation factor X.

Abstract:

: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.

authors

Fung MR,Hay CW,MacGillivray RT

doi

10.1073/pnas.82.11.3591

subject

Has Abstract

pub_date

1985-06-01 00:00:00

pages

3591-5

issue

11

eissn

0027-8424

issn

1091-6490

journal_volume

82

pub_type

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