New Neutral Amino Acids Findings Reported from University of North Colorado [Characterization, mechanism of anticoagulant action, and assessment of therapeutic potential of a fibrinolytic serine protease (Brevithrombolase) purified from ...]
By a News Reporter-Staff News Editor at Biotech Week -- Current study results on Neutral Amino Acids have been published. According to news reporting out of Greeley, Colorado, by NewsRx editors, research stated, "In this study, biochemical and pharmacological characterization of Brevithrombolase, a fibrinolytic serine protease purified from Brevibacillus brevis strain FF02B has been reported. An assessment of its thrombolytic potency has also been made."
Our news journalists obtained a quote from the research from the University of North Colorado, "The molecular mass of this monomeric protease was determined as 55 kDa, and 56043 Da, respectively, by SDS-PAGE and MALDI-TOF-MS. In the analytical studies, the N-terminal sequence of Brevithrombolase was found to be blocked; however, the peptide mass fingerprinting and amino acid composition analyses demonstrated the similarity of Brevithrombolase with endopeptidases in possessing serine in their catalytic triad. This finding was confirmed by the observation that the serine protease inhibitors decrease the catalytic (fibrinolytic) activity of Brevithrombolase. The secondary structure of Brevithrombolase was composed of 30.6% alpha helix and 69.4% random coil. Brevithrombolase showed the Km and Vmax values towards the chromogenic substrate for plasmin at 0.39 mM and 14.3 mu mol/min, respectively. Brevithrombolase demonstrated optimum fibrinolytic activity at pH 7.4 and 37 degrees C, and showed marginal hydrolytic activity towards globulin, casein and fibrinogen. The anticoagulant potency of Brevithrombolase was comparable to the low molecular mass heparin/antithrombin-III and warfarin. Among the three enzymes-Brevithrombolase, plasmin and streptokinase-the fibrinolytic activity and in vitro thrombolytic potency of Brevithrombolase was found to be superior. The RP-HPLC and SDS-PAGE analyses suggested a similar pattern of fibrin degradation by Brevithrombolase and plasmin, indicating that former enzyme is a plasmin-like fibrinolytic serine protease. Brevithrombolase did not show in vitro cytotoxicity on HT29 and HeLa cells or hemolytic activity. At a dose of 10 mg/kg, Brevithrombolase did not exhibit lethality or toxicity on Wistar strain albino rats. Brevithrombolase did not inhibit factor Xa, and its mechanism of anticoagulant action was associated with the enzymatic cleavage of thrombin."
According to the news editors, the research concluded: "The combined properties of Brevithrombolase indicate its therapeutic potential in peptide-based cardiovascular drug development."
For more information on this research see: Characterization, mechanism of anticoagulant action, and assessment of therapeutic potential of a fibrinolytic serine protease (Brevithrombolase) purified from Brevibacillus brevis strain FF02B. Biochimie, 2014;103C():50-60. Biochimie can be contacted at: Elsevier France-Editions Scientifiques Medicales Elsevier, 23 Rue Linois, 75724 Paris, France. (Elsevier - www.elsevier.com; Biochimie - www.elsevier.com/wps/product/cws_home/505803)
Our news journalists report that additional information may be obtained by contacting S. Majumdar, Univ No Colorado, Sch Biol Sci, Greeley, CO 80639, United States. Additional authors for this research include B. Sarmah, D. Gogoi, S. Banerjee, S.S. Ghosh, S. Banerjee, P. Chattopadhyay and A.K. Mukherjee (see also Neutral Amino Acids).
Keywords for this news article include: Greeley, Therapy, Colorado, Angiology, Thrombolytic, United States, Serine Proteases, Peptide Hydrolases, Neutral Amino Acids, Enzymes and Coenzymes, North and Central America
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