CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from <Emphasis Type="Italic">Crotalus atrox</Emphasis> venom |
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Authors: | Montamas Suntravat Paul R Langlais Elda E Sánchez Vance G Nielsen |
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Institution: | 1.Department of Chemistry, National Natural Toxins Research Center,Texas A&M University-Kingsville,Kingsville,USA;2.The Department of Medicine, Division of Endocrinology,University of Arizona College of Medicine,Tucson,USA;3.The Department of Anesthesiology,University of Arizona College of Medicine,Tucson,USA |
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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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