| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10881644 | Toxicon | 2005 | 18 Pages |
Abstract
Snake venom glands synthesize a variety of serine proteinases capable of affecting the haemostatic system. They act on macromolecular substrates of the coagulation, fibrinolytic, and kallikrein-kinin systems, and on platelets to cause an imbalance of the haemostatic system of the prey. In this review we describe their biochemical/biophysical characteristics, biological activities as well as aspects of their evolution and structure-activity relationship.
Keywords
p-nitrophenyl p-guanidinobenzoateTPCKPPACKTLCKSnake Venom Serine proteinasesATIIIPAI-1SBTIdiisopropylfluorophosphateBPTIADPPMSFDAPIt-PADFPNPGBε-ACAUTRFBGmAb4',6-diamidino-2-phenylindoleu-PAε-aminocaproic acidadenosine diphosphateFREMonoclonal antibodyantithrombin IIIPlatelet-aggregationmolecular recognitionParTissue-type plasminogen activatorurokinase plasminogen activatorphenylmethylsulfonyl fluorideFibrinogenBlood clottingMolecular modelinguntranslated regionplasminogen activator inhibitor 1soybean trypsin inhibitorprotease activated receptor
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry, Genetics and Molecular Biology (General)
Authors
Solange M.T. Serrano, Rachid C. Maroun,