ACETYLCHOLINESTERASE OF BUNGARUS-MULTICINCTUS VENOM - PURIFICATION AND PROPERTIES

  • 1 January 1979
    • journal article
    • research article
    • Vol. 34  (1-2) , 27-32
Abstract
Acetylcholinesterase from banded krait (B. multicinctus) venom was purified by CM-Sephadex chromatography and affinity chromatography to a specific activity of 4290 U/mg. The purified enzyme is a glycoprotein. It is free of electrophoretically detectable contaminating proteins. A MW of 140,000 .+-. 5000 was determined by gradient gel electrophoresis for the native enzyme. It is split into 2 equal-sized subunits (MW 70,000 .+-. 2000) by sodium dodecyl sulfate treatment. The N-terminal amino acid analysis gave glycine and serine. The purified acetylcholinesterase can be resolved by disc gel electrophoresis into 4 and by isoelectric focusing into 6 isozymes. The pI [isoelectric point] value of the main isozyme was 5.98 .+-. 0.05.

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