Purification of a proteolytic enzyme from the venom of bothrops brazili snake and study of its activity on fibrinogen

Maria Azanero, Enrique Escobar, Armando Yarleque

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Abstract

© Facultad de Ciencias Bioĺgicas UNMSM. A proteolitic enzyme was purified from Bothrops brazili Peruvian snake venom using Sephadex G- 100 followed by CM-Sephadex C-50, In both two cases with 0.05M ammonium acetate pH 7,0. The enzyme was purified 3,2 fold with 52,5% of yield and by gel filtration the enzyme showed 18 000 of molecular weight, while the PAGE-SDS showed only on9 protein band of 22 000 in the presence of mercaptoethanol and 20 300 under nonreducing conditions which suggests that the enzyme has a single polypeptide chain with disulfide bond. The enzyme hydrolizes fibrinogen, fibrin, casein and afbucnin, but not hemoglobin. and mioglobin. The enzyme is a Aa-fibrinogenase because preferentially hydrolizes the Aa chain of the fibrinogen molecule. This activity is inhibited by EDTA hut not by PMSF, TLCK, iodoacstate and pepstatin, suggests that is a metalloproteinase, however the ions Ca+-+, Mg++ and Zn+f cannot reactivate the inhibition by EDTA. Finally the enzyme is stable up to 45 °C and in its effect on fibrin the enzyme is to attack a chain rapidly.
Original languageAmerican English
Pages (from-to)55-66
Number of pages12
JournalRevista Peruana de Biologia
StatePublished - 1 Jan 2000

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