{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Thakur S"],"funding":["Department of Biotechnology"],"pagination":["201"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11054993"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(4)"],"pubmed_abstract":["Green pit viper bites induce mild toxicity with painful local swelling, blistering, cellulitis, necrosis, ecchymosis and consumptive coagulopathy. Several bite cases of green pit vipers have been reported in several south-east Asian countries including the north-eastern region of India. The present study describes isolation and characterization of a haemostatically active protein from <i>Trimeresurus erythrurus</i> venom responsible for coagulopathy. Using a two-step chromatographic method, a snake venom serine protease erythrofibrase was purified to homogeneity. SDS-PAGE of erythrofibrase showed a single band of ~30 kDa in both reducing and non-reducing conditions. The primary structure of erythrofibrase was determined by ESI LC-MS/MS, and the partial sequence obtained showed 77% sequence"],"journal":["Toxins"],"pubmed_title":["Isolation and Functional Characterization of Erythrofibrase: An Alfa-Fibrinogenase Enzyme from &lt;i&gt;Trimeresurus erythrurus&lt;/i&gt; Venom of North-East India."],"pmcid":["PMC11054993"],"funding_grant_id":["BT/PR24531/ NER/95/755/2017"],"pubmed_authors":["Lalremsanga HT","Santra V","Doley R","Thakur S","Malhotra A","Giri S","Yasmin R"],"additional_accession":[]},"is_claimable":false,"name":"Isolation and Functional Characterization of Erythrofibrase: An Alfa-Fibrinogenase Enzyme from &lt;i&gt;Trimeresurus erythrurus&lt;/i&gt; Venom of North-East India.","description":"Green pit viper bites induce mild toxicity with painful local swelling, blistering, cellulitis, necrosis, ecchymosis and consumptive coagulopathy. Several bite cases of green pit vipers have been reported in several south-east Asian countries including the north-eastern region of India. The present study describes isolation and characterization of a haemostatically active protein from <i>Trimeresurus erythrurus</i> venom responsible for coagulopathy. Using a two-step chromatographic method, a snake venom serine protease erythrofibrase was purified to homogeneity. SDS-PAGE of erythrofibrase showed a single band of ~30 kDa in both reducing and non-reducing conditions. The primary structure of erythrofibrase was determined by ESI LC-MS/MS, and the partial sequence obtained showed 77% sequence","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-04-24T03:16:08.535Z","creation":"2026-04-24T03:09:42.742Z"},"accession":"S-EPMC11054993","cross_references":{"pubmed":["38668626"],"doi":["10.3390/toxins16040201"]}}