Abstract
A fibrinolytic enzyme with a molecular weight between 23 000 and 25 000 Da has been purified from southern copperhead snake venom. Immobilized pH gradient isoelectric focusing with an ultranarrow pH interval (pH 6.65–6.95) resolved two isoforms of the fibrinolytic enzyme that were not resolved by standard isoelectric focusing. Attempts at purification of the individual isoenzymes by semi-preparative scale IPG and elution of enzyme by macerating the gel yielded only 20–40% recovery of activity. In attempts to improved recovery, a semi-preparative IPG canal-isoelectric focusing technique has been utilized.
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