Purification and Characterization of a Novel Fibrinolytic Protease from Schizophyllum commune
Resource
JOURNAL OF FOOD AND DRUG ANALYSIS, 18(2), 69-76
Journal
JOURNAL OF FOOD AND DRUG ANALYSIS
Journal Volume
18
Journal Issue
2
Pages
69-76
Date Issued
2010
Date
2010
Author(s)
Lu, Chung-Lun
Chen, Sherwin
Chen, Shiu-Nan
Abstract
A fibrinolytic enzyme of the mushroom, Schizophyllum commune was purified with chromatographic methods, including a DEAE-Sephadex A-50 ion-exchange column and gel filtrations with Sephadex G-75 and Sephadex G-50 columns. The analysis of fibrin-zymography and SDS-PAGE showed that the enzyme was a monomeric subunit that was estimated to be approximately 17 kDa in size. The fibrinolytic activity of the enzyme in plasminogen-rich and plasminogen-free fibrin plates was 1.25 and 0.44 U/ml, respectively. The N-terminal amino acid sequence of the purified enzyme was identified as HYNIXNSWSSFID, which was highly distinguished from known fibrinolytic enzymes. The relative activity of the purified enzyme with an addition of 5 mM EDTA, Phosphoramidon, and Bestatin was about 76, 64, and 52%, respectively, indicating that it is a metalloprotease. The optimum temperature for the purified enzyme was approximately 45°C, and over 87% of the enzymatic activity was maintained as a stable state in a pH range from 4.0 to 6.0. Therefore, our results suggest that the potential thrombolytic agent from S. commune is a unique type of fibrinolytic enzyme.
Type
journal article
File(s)![Thumbnail Image]()
Loading...
Name
126.pdf
Size
23.19 KB
Format
Adobe PDF
Checksum
(MD5):88a295325e2835b2b8e4b741a2af2440