Abstract
It has been recently demonstrated that the hemotoxic venom activity of several species of snakes can be inhibited by carbon monoxide (CO) or a metheme forming agent. These and other data suggest that the biometal, heme, may be attached to venom enzymes and may be modulated by CO. A novel fibrinogenolytic metalloproteinase, named CatroxMP-II, was isolated and purified from the venom of a Crotalus atrox viper, and subjected to proteolysis and mass spectroscopy. An ion similar to the predicted singly charged m/z of heme at 617.18 was identified. Lastly, CORM-2 (tricarbonyldichlororuthenium (II) dimer, a CO releasing molecule) inhibited the fibrinogenolytic effects of CatroxMP-II on coagulation kinetics in human plasma. In conclusion, we present the first example of a snake venom metalloproteinase that is heme-bound and CO-inhibited.
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Citations
Feb 10, 2019·Toxins·Vance G NielsenSam Afshar
May 28, 2019·Journal of Thrombosis and Thrombolysis·Vance G Nielsen
Aug 16, 2019·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·Vance G NielsenBrian J Turchioe
Aug 23, 2018·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Vance G Nielsen, Nathaniel Frank
Aug 12, 2018·Toxins·Vance G. NielsenRyan W Matika
Aug 9, 2018·Human & Experimental Toxicology·V G Nielsen, N Frank
Nov 5, 2019·Journal of Thrombosis and Thrombolysis·Vance G Nielsen
Apr 8, 2019·Journal of Thrombosis and Thrombolysis·Vance G Nielsen, Nathaniel Frank
May 1, 2021·International Journal of Molecular Sciences·Vance G Nielsen
Jun 3, 2021·Toxins·Anant DeshwalSuresh Kumar Thallapuranam