| pubmed-article:7324533 | pubmed:abstractText | Membrane bound, Triton X-100 solubilized bovine nucleus caudatus acetylcholinesterase is sedimenting in presence of Triton X-100 concentrations higher than the CMC as a 10.5 S-detergent-enzyme complex. There is evidence that this complex does neither represent the molecular enzyme arrangement present in the membrane, nor the molecular form originally released from the membrane. The purified, cytoplasmatic acetylcholinesterase is sedimenting as a 10.5 S-form too. This form is clearly to be distinguished from the detergent enzyme complex, for it is obviously not capable of aggregating, whereas the 10.5 S-detergent-enzyme complex aggregates on detergent removal to defined water soluble oligomers with sedimentation coefficients of 16 S (700 000 +/- 10 000), 20.6 S (960 000 +/- 60 000) and 23.3 S (approximately 1 200 000). In contrast to acetylcholinesterase from erythrocytes this aggregation is not easily reversibly by incubation with Triton X-100, reflecting differences in the hydrophobic part of the enzymes. Purified acetylcholinesterase solubilized without detergent under autolytic or tryptic conditions is mainly sedimenting as a 4.5 S-form. Such slow sedimenting forms detected in crude solubilisates of neuronal tissues, may originate at least partially form autolytic solubilization. | lld:pubmed |
