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  • Title: Molecular forms of purified human erythrocyte membrane acetylcholinesterase investigated by crosslinking with diimidates.
    Author: Römer-Lüthi CR, Hajdu J, Brodbeck U.
    Journal: Hoppe Seylers Z Physiol Chem; 1979 Jul; 360(7):929-34. PubMed ID: 488916.
    Abstract:
    Several molecular forms of human erythrocyte membrane acetylcholinesterase have been studied after crosslinking with bifunctional diimidates. The crosslinked products were analysed by centrifugation on linear sucrose density gradients containing Triton X-100. Molecular weights of covalently linked oligomers were estimated by sodium dodecylsulfate gel electrophoresis. It was shown that acetylcholinesterase crosslinked in absence of Triton X-100 consists of molecular forms built up by dimeric protomers. These dimers were identical with the enzymatically active species sedimenting with 6.5S in linear sucrose density gradients.
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