{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,14]],"date-time":"2026-08-14T17:31:15Z","timestamp":1786728675201,"version":"build-2736575974"},"reference-count":31,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"2","license":[{"start":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T00:00:00Z","timestamp":1740787200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/4.0"}],"content-domain":{"domain":["lww.com","ovid.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2025,3]]},"abstract":"<jats:sec>\n                    <jats:title>Background and purpose:<\/jats:title>\n                    <jats:p>\n                      Snake venom contains numerous proteolytic enzymes, including metalloproteases. This study aimed to isolate, characterize the metalloproteinase from\n                      <jats:italic toggle=\"yes\">Montivipera raddei<\/jats:italic>\n                      venom and insert its cDNA into a host cell genome for expressing the protein's potential use as a coagulation factor.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Experimental approach:<\/jats:title>\n                    <jats:p>\n                      Initially,\n                      <jats:italic toggle=\"yes\">M. raddei<\/jats:italic>\n                      venom was analyzed using SDS-PAGE and ion-exchange chromatography. All purified fractions were assessed using a prothrombin time (PT) assay. Immunoblot analysis and MALDI-TOF\/TOF MS spectrometry confirmed the metalloproteinase active domain in the obtained fraction. All of the confirmations were studied using the I-TASSER server. To produce the recombinant enzyme, metalloproteinase cDNA was isolated from the total RNA of the Caucasus viper venom gland tissue and cloned into pEX-A2-H plasmid, containing homologous sequences with CHO-S cell genome. Also, it was confirmed by western blotting and PT test.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Findings\/Results:<\/jats:title>\n                    <jats:p>\n                      Two fractions from\n                      <jats:italic toggle=\"yes\">M. raddei<\/jats:italic>\n                      venom had PT values of 6 and 21 s, respectively. We confirmed the presence of a 25-KDa procoagulant metalloprotease (Met). The results indicated successful expression of the Met protein in the recombinant CHO-S cells. The Met protein was structurally similar to the target in the PDB ID. 2e3x, regulatory subunit of the blood coagulation factor X- and IX-activating enzyme. The Met protein also contained a similar binding domain with 60 amino acids, comparable to those in\n                      <jats:italic toggle=\"yes\">E. carinatus<\/jats:italic>\n                      . and\n                      <jats:italic toggle=\"yes\">E. pyramidum leakeyi<\/jats:italic>\n                      metalloproteinases.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusion and implications:<\/jats:title>\n                    <jats:p>The Met protein may be a potent candidate recombinant coagulant drug. Remarkably, the thrombin time for this protein was 3 s.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.4103\/rps.rps_34_24","type":"journal-article","created":{"date-parts":[[2025,3,31]],"date-time":"2025-03-31T02:07:02Z","timestamp":1743386822000},"page":"207-217","update-policy":"https:\/\/doi.org\/10.1097\/lww.0000000000001000","source":"Crossref","is-referenced-by-count":0,"title":["Isolation, characterization, and expression of the Montivipera raddei (Caucasus viper) venom metalloprotease-like protein"],"prefix":"10.4103","volume":"20","author":[{"given":"Zohreh","family":"Jafari","sequence":"first","affiliation":[{"name":"Department of Medical Biotechnology, School of Advanced Technologies in Medicine, Shahid Beheshti University of Medical Sciences, Tehran, I.R. 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