caa a22 4500 37887439X CHVBK 20180305123417.0 cr unu---uuuuu 161128e20030220xx s 000 0 eng 10.1515/BC.2003.024 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.024 A Novel Influenza A Virus Activating Enzymefrom Porcine Lung: Purification andCharacterization [Elektronische Daten] [M. Sato, S. Yoshida, K. Iida, T. Tomozawa, H. Kido, M. Yamashita] Proteolytic activation of hemagglutinin, an envelope glycoprotein of the influenza virus, by host proteases is essential for infection and proliferation of the virus. However, there is no well-defined, inherent source of host proteases in man or swine, both of which are natural hosts for human influenza viruses. We have recently isolated a 32 kDa protein in a high salt extract from porcine lungs, which possess the hemagglutinin processing activity. In this study, we attempted to purify another hemagglutinin processing enzyme from porcine lung. The purified enzyme, named tryptase TC30, exhibited a molecular mass of about 30 kDa by SDS-PAGE and 28.5 kDa by gel filtration chromatography, suggesting that it is a monomer. Tryptase TC30 cleaved peptide substrates with Arg at the P1 position, and preferentially substrates with the Ser-Ile-Gln-Ser-Arg sequence corresponding to the HA cleavage site sequence of the A/PR/8/34 influenza virus. Among various inhibitors tested, trypsintype serine protease inhibitors, such as aprotinin, antipain, benzamidine and leupeptin, efficiently inhibited the proteolytic activity of the enzyme. The N-terminal 40 amino acid sequence of tryptase TC30 exhibits more than 60% homology to mast cell tryptases from mice MCP-6 and human tryptase-α and -β. These data indicate that tryptase TC30, the 30 kDa enzyme from porcine lung, is a novel hemagglutinin-cleaving enzyme. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Sato M. aut Yoshida S. aut Iida K. aut Tomozawa T. aut Kido H. aut Yamashita M. aut Biological Chemistry Walter de Gruyter 384/2(2003-02-20), 219-227 1431-6730 384:2<219 2003 384 bchm https://doi.org/10.1515/BC.2003.024 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.024 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sato M. aut NATIONALLICENCE 700 1- Yoshida S. aut NATIONALLICENCE 700 1- Iida K. aut NATIONALLICENCE 700 1- Tomozawa T. aut NATIONALLICENCE 700 1- Kido H. aut NATIONALLICENCE 700 1- Yamashita M. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/2(2003-02-20), 219-227 1431-6730 384:2<219 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter