Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1948923 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2006 | 7 Pages |
Abstract
The aim of this study was to purify and characterise a novel protease inhibitor (PISC-2002) isolated from culture supernatants of Streptomyces chromofuscus. PISC-2002 was purified by anion-exchange chromatography, and RP-HPLC analysis. PISC-2002 had a molecular mass of 11.2 kDa and a high content of hydrophobic amino acids and proline. N-terminal sequence gave two sequences differing by one residue. The main sequence is ASLPAVSALVLTV and the shorter sequence is SLPAVSALVLTV. This shows its homology to Streptomyces subtilisin inhibitor family. Besides its large spectrum of powerful inhibitory activities against various serine proteases, PISC-2002 displayed significant antiviral effect against influenza virus A/Rostock/34 (H7N7).
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Authors
Lidiya Angelova, Michèle Dalgalarrondo, Ignat Minkov, Svetla Danova, Nicolai Kirilov, Julia Serkedjieva, Jean-Marc Chobert, Thomas Haertlé, Iskra Ivanova,