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Primary structure of the virus activating protease: from chick embryo Its identity with the blood clotting factor Xa
Author(s) -
Suzuki Harukazu,
Harada Atzuko,
Hayashi Yumiko,
Wada Kohji,
Asaka Jun-ichiro,
Gotoh Bin,
Ogasawara Tomohiko,
Nagai Yoshiyuki
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80608-6
Subject(s) - protease , embryo , clotting factor , blood clotting , virology , virus , identity (music) , biology , immunology , chemistry , medicine , genetics , biochemistry , enzyme , physics , acoustics
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.