✦ LIBER ✦

Purification of acetylcholinesterase from pig cerebral cortex by affinity chromatography

✍ Scribed by Charles A. Reavill; David T. Plummer

Publisher: Elsevier Science
Year: 1978
Tongue: English
Weight: 896 KB
Volume: 157
Category: Article
ISSN: 1873-3778
DOI: 10.1016/s0021-9673(00)92330-6

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✦ Synopsis

SUMM.ARY

Acetylcholinesterase from pig cerebral cortex was solubilised with 1% (w/v) . Triton X-l.00 and purified by affinity chromatography. Three different Iigands were investigated and details are given for their preparation. The elution profile depended on the presence of Triton X-100, the ionic strength and the inhibitor used to remove the enzyme from the column as well as the nature of the affinity material.

The most efficient purification was obtained when the enzyme was eluted from a column containing the acetylcholinesterase inhibitor [l-methyl-9-(Nfi-e-aminocaproyl)-#I-aminopropylamino] acridinium bromide hydrobromide covalently linked to Sepharose 4B. A recovery of 44% of the applied enzyme was eluted from the column with a specific activity of 148 ymoles min-' mg-r and a purification of 90fold.

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