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1979 (1)
1Author    H. Großmann, M. W. Einert, M. LiefländerRequires cookie*
 Title    Acetylcholinesterase aus dem Gift von Bungarus multicinctus. Reinigung und Eigenschaften The Acetylcholinesterase of Bungarus multicinctus Venom. Purification and Properties  
 Abstract    Acetylcholinesterase from Banded krait (Bungarus m ulticinctus) venom has been purified by CM -Sephadex chrom atography and affinity chromatography to a specific activity of 4290 U/mg. The purified enzyme is a glycoprotein. It is free of electrophoretically detectable contam inating proteins. A m olecular weight of 140 000 + 5 000 has been determ ined by gradient gel electro­ phoresis for the native enzyme. It is split into two equal-sized subunits (Mr 70 000 + 2 000) by SDS treatm ent. The N -term inal 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 p i value of the m ain isozyme has been found to be 5.98 + 0.05. 
  Reference    Z. Naturforsch. 34c, 27 (1979); eingegangen am 2. November 1978 
  Published    1979 
  Keywords    Acetylcholinesterase, Snake Venom, B ungarus m ulticinctus, Affinity Chromatography, Isozymes 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0027.pdf 
 Identifier    ZNC-1979-34c-0027 
 Volume    34