Acetylcholinesterase aus dem Gift von Bungarus multicinctus. Reinigung und Eigenschaften/The Acetylcholinesterase of Bungarus multicinctus Venom. Purification and Properties

Abstract

Abstract Acetylcholinesterase from Banded krait (Bungarus multicinctus) venom has been 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 molecular weight of 140 000 ± 5 000 has been determined by gradient gel electrophoresis for the native enzyme. It is split into two equal-sized subunits (Mr 70 000 ± 2 000) by SDS treatment. The N-terminal amino acid analysis gave glycine and serine. The purified acetyl­ cholinesterase can be resolved by disc gel electrophoresis into four and by isoelectric focusing into six isozymes. The pI value of the main isozyme has been found to be 5.98 ± 0.05.