Characterization of a proteolytic enzyme from Lachesis muta venom (Serpentes: Viperidae).
A proteolytic enzyme from L. muta stenophrys was isolated by gel filtration on Bio Gel P-100 followed by FPLC on MONO S column. The enzyme exhibited proteolytic activity toward casein, hemoglobin and fibrinogen with a pH optimum around 10. The activity was inhibited by EDTA while trypsin inhibitors were not inhibitory. It is a glycoprotein, Mr 14 kDa with a high content of Asp, Glu, and Leu residues and a low content of Cys and Trp. The protease is devoid of myotoxic, hemorrhagic, esterolytic and amidolytic activities. It lyses the alfa and beta chains of human fibrinogen and releases kinin from L.M.W. kininogen. No release of histamine was observed upon incubation with mast cells.
Aragón-Ortiz
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Departamento de Bioquímica, Universidad de Costa Rica.
D000818:Animals; D002850:Chromatography, Gel; D003435:Crotalid Venoms / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D011480:Protease Inhibitors / Q000494:pharmacology
D003435:Crotalid Venoms; D011480:Protease Inhibitors; D010447:Peptide Hydrolases