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M Weinert

Publications and source records attributed to M Weinert.

69 records · Page 4Linked to original sources
PubMed1976

[Large scale purification of the acetylcholinesterase from bovine caudate nucleus by affinity chromatography (author's transl)].

The acetylcholinesterase from bovine caudate nucleus was solubilized with 0.6-0.8% Triton X-100. It was purified and freed from Triton X-100 by means of a two-fold affinity chromatography procedure. A simple three-step synthesis of the inhibitor with attached spacer arm used in affinity chromatography is described. Starting from 3 kg of caudate nucleus, nearly 11 mg of the purified acetylcholinesterase with a spec. act of 4250 U/mg (13 500-fold purification) could be obtained in an over-all yield of 49%. On gel electrophoresis the enzyme produces several enzymatically active glycoproteinbands of oligomeres. On sodium dodecylsulfate gel electrophoresis in the presence of a disulfide-reducing agent it yields a molecular weight of 72000 +/- 2000 for the smallest subunit. In the absence of a disulfide-reducing agent a band for a dimer besides the band for the monomer could be detected and a molecular weight of 142000 +/- 3000 was estimated for this species.

Acetylcholinesterase↗
PubMedDate not supplied

[The acetylcholinesterase of Bungarus multicinctus venom. Purification and properties (author's transl)].

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 acetylcholinesterase 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.

Acetylcholinesterase↗