Almost complete removal of the deter-aggregates, which contained small amounts of gent from a purified 10.7 S complex consisting of bound residual Triton X-100 in the range of acetylcholinesterase and [ 3 H]Triton X-100 bound 0.4-1.6 mol Triton X-100 per mol acetylcholinto an affinity gel was achieved by extensive esterase. Besides these aggregates, a nearly deterwashing and subsequent elution of the enzyme. gent-free 10.5S form was observed, lacking the Applying this procedure of detergent removal, hydrophobic region responsible for detergent the majority of the enzyme could be stabilized binding and self-aggregation, by self-aggregation forming soluble 16S and 20 S
Nachweis und Trennung von globulären hydrophoben und nicht hydrophoben Formen der Acetylcholinesterase aus dem Nucleus caudatus vom RindZusammenfassung: Der gereinigte, an ein Affini-20S-Aggregate, die noch geringe Reste von getätsgel gebundene 10.7S-Komplex bestehend aus bundenem Triton X-100 im Bereich von 0.4-1.6 Acetylcholinesterase und [ 3 H]Triton X-100 wur-mol Triton X-100 pro mol Acetylcholinesterase de durch mehrere Waschvorgänge und nachfolenthalten. Neben diesen Aggregaten wurde auch gende Elution fast vollständig vom Detergenz be-eine nahezu detergenzfreie 10.SS-Form nachgefreit. Wird das Detergenz auf diese Weise entfernt, wiesen, der die hydrophoben Bereiche, die sokann sich das Enzym durch Selbstaggregation wohl für die Detergenzbindung als auch die stabilisieren. Dabei entstehen lösliche 16S-und Selbstaggregation nötig sind, fehlen.
The number of catalytic subunits of purified bovine nucleus caudatus acetylcholinesterase (E.C. 3.1.1.7) has been determined by active site labelling with [3H]diisopropyl fluorophosphate ([3H]DFP). The 10.5 S, 16 S, and 20 S forms were estimated to contain two, four, and six active sites, respectively, per molecule. A 4.8 S form, which showed a weak amphiphile-dependent activity behavior, was obtained by selective proteolytic digestion with pronase. The inability of the purified 4.8 S form to aggregate after detergent removal, and the molecular mass in the range of 130-165 kD under nondenaturating conditions, indicate that this form is a dimeric form, lacking those hydrophobic regions responsible for aggregation.
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