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Our news editors obtained a quote from the research, "This purification protocol resulted 80.9-fold purification of the enzyme and a final yield of 5.7%. The molecular weight of the purified enzyme was estimated to be 21 kDa by SDS-PAGE and size exclusion gel filtration. The N-terminal amino acid sequence was found to be ITFQSASP, which is dissimilar from that of known fibrinolytic enzymes. The purified enzyme was a neutral protease with an optimal reaction pH and temperature of 8.0 and 37 degrees C, respectively. Enzymatic activity was inhibited by Cu2+ and Co2+. It was also significantly inhibited by PMSF and TPCK. Furthermore, it was found to exhibit a higher specificity for S-7388, a well-known chymotrypsin chromogenic substrate, indicating chymotrypsin like serine metalloprotease. The relative fibrinolytic activity of 5 mu g purified enzyme have two fold more activity than 1 unit/ml of plasmin on fibrin plate. Furthermore, purified enzyme preferentially hydrolyzed the A alpha-chain followed by the B beta- and gamma-chain of fibrinogen, which is precursor of fibrin."
According to the news editors, the research concluded: "Therefore, these data suggests that the fibrinolytic enzyme derived from edible mushroom, L. shimeji, might be useful for thrombolytic therapy and preventing thrombotic disease."
For more information on this research see: Purification and characterization of a novel fibrinolytic alpha chymotrypsin like serine metalloprotease from the edible mushroom, Lyophyllum shimeji.
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