Purification,characterization and substrate specificity of a basic proteinase in the venom of Habu (Trimeresurus flavoriridis) |
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| Institution: | 1. College of Pharmacy, Research Institute of Pharmaceutical Sciences, Kyungpook National University, Daegu 41566, Republic of Korea;2. College of Pharmacy, Chungnam National University, Daejon 34134, Republic of Korea;1. Department of Biological Science and Technology, National Pingtung University of Science and Technology, No. 1, Shuefu Road, Pingtung, 912301, Taiwan;2. Institute of Biological Chemistry, Academia Sinica, No. 128, Academia Road Sec. 2, Taipei, 115, Taiwan;3. Institute of Biochemical Sciences, National Taiwan University, No. 1, Sec. 4, Roosevelt Rd., Taipei, 106319, Taiwan;4. Department of Medical Research, Taipei Veterans General Hospital, No. 322, Sec. 2, Shipai Rd., Taipei, 112062, Taiwan;5. Department of Biology and Anatomy, National Defense Medical Centre, No. 161, Sec. 6, Minquan E. Rd., Taipei, 11490, Taiwan;1. Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia;2. CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France;3. VenomeTech, 473 Route des Dolines – Villa 3, 06560 Valbonne, France;4. Laboratoire Écologie Fonctionnelle et Environnement, Université de Toulouse, 118 Route de Narbonne, 31062 Toulouse, France |
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| Abstract: | A basic proteinase was purified and characterized from the venom of Habu (Trimeresurus flavoviridis). Its molecular weight, isoelectric point and optimum pH were approx. 24 000, 9.2 and 9, respectively. Susceptibility to several reagents was examined. The proteinase had endopeptidase activity cleaving the Gly-Leu bond in synthetic peptides but no exopeptidase activity. It did not hydrolyze a peptide, Z-Gly-Pro-Leu-Gly-Pro, which had been a good substrate for the major proteinase in the venom. The proteinase cleaved oxidized insulin B chain at five positions: His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Gly23-Phe24 and Phe24-Phe25. From the disappearance of intermediate peptides and the peptides accumulated, the order and the intensity of cleavage of these positions were determined, and the substrate specificity was compared with those hitherto described for hemorrhagic and nonhemorrhagic venom proteinases. |
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