Please use this identifier to cite or link to this item: https://idr.l2.nitk.ac.in/jspui/handle/123456789/9669
Title: A novel fibrinolytic serine metalloprotease from the marine Serratia marcescens subsp. sakuensis: Purification and characterization
Authors: Krishnamurthy, A.
Belur, P.D.
Issue Date: 2018
Citation: International Journal of Biological Macromolecules, 2018, Vol.112, , pp.110-118
Abstract: This study demonstrates the purification and characterization of a fibrinolytic serine metalloprotease from the marine Serratia marcescens subsp. sakuensis (KU296189.1). The purified enzyme (1033 U/mg) had a molecular weight of 43 KDa, with optimum pH and temperature being 7 and 55 C. The in vitro half-life of the fibrinolytic enzyme at 37 C was found to be 19 h. The kinetic constants, Km and Vmax of the purified enzyme determined using fibrin as substrate was 0.66 mg/mL and 158.73 U/mL. The Kcat and catalytic efficiency of the enzyme was found to be 12.21 min?1 and 18.32 mL/(mg min) respectively. The fibrinolytic enzyme did not show any proteolytic activity towards blood plasma proteins like haemoglobin, ?-globulins and transferrin. In vitro studies revealed that the fibrinolytic enzyme displayed 38% clot lysis for a period of 3 h which was higher than that displayed by streptokinase and heparin. A total of seven peptide sequences were obtained after the LC-MS/MS-TOF analysis, out of which only four sequences showed 67% homology with the sequences of the other proteases. All these results suggest its novelty and potential application in thrombolytic therapy. 2018 Elsevier B.V.
URI: 10.1016/j.ijbiomac.2018.01.129
http://idr.nitk.ac.in/jspui/handle/123456789/9669
Appears in Collections:1. Journal Articles

Files in This Item:
File Description SizeFormat 
7.A novel fibrinolytic serine.pdf1.3 MBAdobe PDFThumbnail
View/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.