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PMID: 2582420 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 82 ·No. 11 ·1985-06-00 ·Pages 3591-5

Fung MR, Hay CW, MacGillivray RT

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cattle DNA/analysis DNA Restriction Enzymes/metabolism Factor X/genetics Humans Poly A/analysis RNA/analysis RNA, Messenger/analysis
Chemicals
RNA, Messenger Poly A RNA Factor X DNA DNA Restriction Enzymes
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Fung M R
Hay C W
MacGillivray R T
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38 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.82.11.3591
Published
1985-06-00
Pages
3591-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC397831
Subset
IM
Databases
GENBANK
K03194
External Links
PubMed source DOI: 10.1073/pnas.82.11.3591 PMC Full Text View journal details
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