Characterization of a proteolytic enzyme from Lachesis muta venom (Serpentes: Viperidae)
Rev. biol. trop
; 40(2): 209-213, Ago. 1992.
Article
in En
| LILACS
| ID: lil-321780
Responsible library:
BR1.1
ABSTRACT
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.
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Index:
LILACS
Main subject:
Peptide Hydrolases
/
Crotalid Venoms
Limits:
Animals
Language:
En
Journal:
Rev. biol. trop
Journal subject:
BIOLOGIA
/
MEDICINA TROPICAL
Year:
1992
Type:
Article