Purification and characterization of two high molecular mass snake venom metalloproteinases (P-III SVMPs), named SV-PAD-2 and HR-Ele-1, from the venom of Protobothrops elegans (Sakishima-habu). (1st September 2015)

• Record Type: Journal Article
• Authors: Oyama, Etsuko; Takahashi, Hidenobu
• Is Part Of: Toxicon. Volume 103(2015)
• Page Start: 30
• Page End: 38
• Publication Date: 2015-09-01
• Subjects: Snake venom -- Metalloproteinases -- Anti-coagulant; Toxins -- Periodicals; Venom -- Periodicals; 615.9
• DOI: 10.1016/j.toxicon.2015.06.010
• Languages: English
• ISSNs: 0041-0101

Abstract

Abstract: We herein identified two high molecular mass metalloproteinases, named SV-PAD-2 and HR-Ele-1, in the venom of Protobothrops elegans . HR-Ele-1 appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) regard under reducing and non-reducing conditions, and the molecular mass of this protease was approximately 60 kDa under reducing conditions. On the other hand, the molecular masses of SV-PAD-2 on SDS-PAGE were 110 kDa under the non-reducing condition and 52 kDa under the reducing condition. These SVMPs exhibited fibrinogenolytic and enzymatic activities against synthetic substrates for matrix metalloproteinases (MMPs) and the insulin B-chain, and were both inhibited by EDTA. SV-PAD-2 inhibited ADP- and collagen-induced platelet aggregation, with IC50 values of 240 nM and 185 nM, respectively. HR-Ele-1 exhibited hemorrhagic activity, and its minimum hemorrhagic dose (MHD) was 0.05 μg in the guinea pig. Highlights: We isolated two P-III SVMPs from Protobothrops elegans venom. SV-PAD-2 was P-IIIc metalloproteinase which inhibits the platelet aggregation, and dissociates ADP-induced platelet aggregation. HR-Ele-1 exhibits hemorrhagic activity.