[Acetylcholinesterase from bovine erythrocytes. Purification and properties of the enzyme solubilized in the presence and the absence of Triton X-100 (author's transl)].

Acetylcholinesterase was released from bovine erythrocytes by Triton X-100 treatment and purified by twwfold affinity chromatography. The detergentfree enzyme was obtained with a specific activity of 4130 U/mg (303 000-fold purification) and a 25% yield. Alternatively, the commercial available crude enzyme was purified. The latter preparation has an uniform molecular weight (Mr 175 000). The Triton-solubilized enzyme, however, can be resolved after removal of the detergent in eight multiple forms (Mr 175 000 and multiple values), in the presence of Triton there exists only one form (Mr 338 000). The amino acid composition of the two enzyme preparations differs significantly. No differences were observed with respect to other properties: SDS gel electrophoresis revealed two protein bands (Mr 166 000 and 86 000) with both preparations. The enzyme is a glycoprotein with a pI value of 4.3 and contains strongly bound phosphatidylethanolamine. The N-terminal amino acid has been found to be Glu (or Gln).