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)》.pdf

Toxicon 103 (2015) 30e38 Contents lists available at ScienceDirect Toxicon journal homepage: /l ocate/toxicon 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) Etsuko Oyama a, *, Hidenobu Takahashi b a Department of Hygienic Chemistry, Meiji Pharmaceutical University, Japan b Meiji Pharmaceutical University, Japan a r t i c l e i n f o a b s t r a c t Article history: We herein identified two high molecular mass metalloproteinases, named SV-PAD-2 and HR-Ele-1, in the Received 23 March 2015 venom of Protobothrops elegans. HR-Ele-1 appeared as a single band on sodium dodecyl sulfate- Received in revised form polyacrylamide gel electrophoresis (SDS) regard under reducing and non-reducing conditions, 8 June 2015 and the molecular mass of this protease was approximately 60 kDa under reducing conditions. On the Accepted 8 June 2015 other hand, the molecular masses of SV-PAD-2 on SDSwere 110 kDa under the non-reducing Available online 19 June 2015 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 Keywords: Snake venom