Purification and characterization of a fibrinolytic enzyme from venom of the southern copperhead snake (Agkistrodon contortrix contortrix).
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Fibrolase is a zinc metalloproteinase containing 1 mol of zinc per mol of protein
"However, the enzyme is a metalloproteinase since it is inhibited by EDTA, o-phenanthroline and tetraethylenepentamine (a specific zinc chelator). Metal analysis revealed 1 mol of zinc/mol of protein."
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Fibrolase exhibits substrate specificity similar to other snake venom metalloproteinases with preference for X-Leu bonds
"Study of cleavage site preference of the fibrinolytic enzyme using the oxidized B chain of insulin revealed that specificity is similar to other snake venom metalloproteinases with cleavage primarily directed to an X-Leu bond."
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Fibrolase exhibits direct fibrinolytic activity without activating plasminogen
"The enzyme exhibits direct fibrinolytic activity and does not activate plasminogen. In vitro studies revealed that fibrolase dissolves clots made either from purified fibrinogen or from whole blood."
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Fibrolase has molecular weight of 23,000-24,000 Da and isoelectric point of pH 6.8
"The enzyme, fibrolase, has a molecular weight of 23,000-24,000 and an isoelectric point of pH 6.8."
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Fibrolase is composed of approximately 200 amino acids with blocked NH2-terminus and contains little or no carbohydrate
"It is composed of approximately 200 amino acids, possesses a blocked NH2-terminus and contains little or no carbohydrate."
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Unlike some other venom fibrinolytic metalloproteinases, fibrolase exhibits little or no hemorrhagic activity
"Interestingly, unlike some other venom fibrinolytic metalloproteinases, fibrolase exhibits little if any hemorrhagic activity."
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Fibrolase is not inhibited by serine protease inhibitors but is specifically inhibited by metal chelators
"The enzyme shows no activity against a series of chromogenic p-nitroanilide substrates and is not inhibited by diisopropylfluorophosphate, soybean trypsin inhibitor, Trasylol, or p-chloromercuribenzoate. However, the enzyme is a metalloproteinase since it is inhibited by EDTA, o-phenanthroline and tetraethylenepentamine (a specific zinc chelator)."