PRIMARY STRUCTURE OF THE VIRUS ACTIVATING PROTEASE FROM CHICK-EMBRYO - ITS IDENTITY WITH THE BLOOD-CLOTTING FACTOR-XA

被引:22
作者
SUZUKI, H
HARADA, A
HAYASHI, Y
WADA, K
ASAKA, J
GOTOH, B
OGASAWARA, T
NAGAI, Y
机构
[1] NAGOYA UNIV, SCH MED, DIS MECHANISM & CONTROL RES INST, NAGOYA, AICHI 466, JAPAN
[2] SHIONOGI INST MED SCI, OSAKA 566, JAPAN
来源
FEBS LETTERS | 1991年 / 283卷 / 02期
关键词
VIRUS ACTIVATING PROTEASE; FACTOR-X; STUART FACTOR; CHICK EMBRYO;
D O I
10.1016/0014-5793(91)80608-6
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
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页码:281 / 285
页数:5
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