Isolation and Characterization of a Novel Elastase Inhibitor, AFLEI from Aspergillus flavus
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A novel elastase inhibitor from <i>Aspergillus flavus</i> (AFLEI) was isolated, and biochemical properties of AFLEI were examined. Column chromatography using diethylaminoethyl (DE) 52-Cellulose and Sephadex G-75 was used to purify the inhibitor. The final preparation was found to be homogeneous as indicated by a single band after disc polyacrylamide gel (PAGE) and isoelectric focusing electrophoreses. AFLEI had a molecular weight of 7,525.8 as determined by TOF-MS (time of flight mass spectrometry). The elastolytic activity of elastases from <i>A. flavus</i>, <i>A. fumigatus</i> and human leukocytes were inhibited by AFLEI. However, this activity from porcine pancreas elastase, trypsin, chymotrypsin, thrombin, and Ac<sub>1</sub>-Proteinase from snake venom was not affected by AFLEI. The fibrinogenase activity of the elastase from <i>A. flavus</i> was inhibited by AFLEI. AFLEI was inhibited by α<sub>2</sub>-macroglobulin. However, ethylenediaminetetraacetic acid (EDTA-2Na), benzamidine, chymostatin, tosyl phenylalanine chloromethyl ketone (TPCK) and dithiothreitol (DTT) did not show any inhibitory effect on the elastase inhibitory activity of AFLEI.
- Japanese Journal of Medical Mycology
Japanese Journal of Medical Mycology 47(3), 219-224, 2006-07-31
The Japanese Society for Medical Mycology