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PMID: 2044767 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Primary structure of the virus activating protease from chick embryo. Its identity with the blood clotting factor Xa.

FEBS letters ·Vol. 283 ·No. 2 ·1991-06-03 ·Pages 281-5

Suzuki H, Harada A, Hayashi Y, Wada K, Asaka J, Gotoh B, Ogasawara T, Nagai Y

Abstract

Host cell proteases activating para- and orthomyxovirus fusion glycoprotein precursors play a crucial role in determining the viral tropism in infected organisms. We previously isolated such an endoprotease from the allantoic fluid of chick embryo and showed its close similarity to the activated form of blood clotting factor X (FXa) by partial amino acid sequencing. In this report, we have cloned and sequenced a cDNA of the protease, and show that it is encoded in a single gene as a preproform with all the functional and structural domains known to be characteristic of bovine or human FX, establishing the identity between the protease and FXa.

MeSH Terms
Allantois/enzymology Amino Acid Sequence Animals Base Sequence Cattle Chick Embryo Chorion/enzymology Cloning, Molecular Enzyme Precursors/genetics Factor Xa/chemistry,genetics Humans Molecular Sequence Data Oligonucleotide Probes Sequence Homology, Nucleic Acid Serine Endopeptidases/chemistry,genetics,isolation & purification
Chemicals
Enzyme Precursors Oligonucleotide Probes Serine Endopeptidases virus activating protease Factor Xa
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Suzuki H
Shionogi Institute for Medical Science, Osaka, Japan.
Harada A
Hayashi Y
Wada K
Asaka J
Gotoh B
Ogasawara T
Nagai Y
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1991-06-03
Pages
281-5
Language
English
Region
England
NLM ID
0155157
Subset
IM
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