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Rapid purification of serine proteinases from Bothrops alternatus and Bothrops moojeni venoms
(Elsevier B.V., 2013-12-15)
Envenomation by Bothrops species results, among other symptoms, in hemostatic disturbances. These changes can be ascribed to the presence of enzymes, primarily serine proteinases some of which are structurally similar to ...
Serine proteinases from Bothrops snake venom activates PI3K/Akt mediated angiogenesis
(2016-12-15)
The discovery of rapid acting and powerful angiogenic proteins are of significant interest in the treatment of various human disorders associated with insufficient angiogenesis such as ischemia, menorrhagia and delayed ...
Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
(2008-01)
A serine proteinase with thrombin-like activity was isolated from the venom of the Central American pit viper Bothrops asper. Isolation was performed by a combination of affinity chromatography on aminobenzamidine-Sepharose ...
Biochemical and biological characterization of two serine proteinases from Colombian Crotalus durissus cumanensis snake venom
(2013-03-01)
Two clotting serine proteinases, named Cdc SI and Cdc SII, were isolated and characterized for the first time from Colombian Crotalus durissus cumanensis snake venom. The enzymes were purified using two chromatographic ...
Membrane independent activation of fibroblast proMMP-2 by snake venom: novel roles for venom proteinases
(2004-12-01)
ProMMP-2 activation by Bothrops asper venom was investigated in mouse gastrocnemius muscle, mammalian cell culture and a cell-free system. Zymography revealed an increment of latent and activated forms of MMP-2 in muscle ...
Purification and primary structure determination of a Bowman-Birk trypsin inhibitor from Torresea cearensis seeds
(Walter De Gruyter & CoBerlinAlemanha, 1997)
Effect of lead, cadmium and zinc on the activity of enamel matrix proteinases in vitro
(Munksgaard Int Publ LtdCopenhagenDinamarca, 2000)
Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases - Crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator
(Amer Soc Biochemistry Molecular Biology Inc, 2005-11-25)
Protein C activation initiated by the thrombin-thrombomodulin complex forms the major physiological anticoagulant pathway. Agkistrodon contortrix contortrix protein C activator, a glycosylated single-chain serine proteinase, ...