Multiple forms of acetylcholinesterase from human erythrocytes.

摘要: 1. Acetylcholinesterase from human erythrocytes was solubilized with Triton X-100 in strong salt solution and partially purified by (NH(4))(2)SO(4) fractionation. This preparation showed three main bands of enzyme activity after electrophoresis on polyacrylamide gel incubation either alpha-naphthyl acetate or acetylthiocholine as substrate. Two the multiple forms were completely inhibited 10mum-eserine one only partially. Treatment neuraminidase had no effect electrophoretic pattern; therefore sialic acid does not appear to determine affect ratios acetylcholinesterase forms, unlike those serum cholinesterase. 2. Chromatography Sephadex G-200 revealed major peak a suggestion two minor zones mol.wt. 546000, 184000 93000 (i.e. proportion 6:2:1). The almost separated overall purification about 600-fold. Further attempts purify absorption calcium phosphate gels unsuccessful. 3. Electrophoresis gradient for 24h that corresponded values molecular weights obtained column chromatography. After 70h further developed making six entities, which simple multiples monomer, thus resembling cholinesterase found serum.