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  • Title: On the homogeneity of 11-S acetylcholinesterase.
    Author: Christopher JP, Kurlansik L, Millar DB, Chignell C.
    Journal: Biochim Biophys Acta; 1978 Jul 07; 525(1):112-21. PubMed ID: 567492.
    Abstract:
    11-S acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) purified by affinity chromatography of trypsin-digested homogenates was shown to be contaminated with three other active forms of enzyme. The initial purification used an affinity column of the inhibitor, N-methylacridinium ion. Chromatography of the "affinity-pure" sample on hydroxyapatite resulted in two peaks of acetylcholinesterase activity. One peak contained only a form sedimenting at 11-S (approx. 85% of the recovered activity). The other peak consisted of a 9.5-S form, in addition to 14-S and 18-S forms. The 9.5-S form (approx. 7% of the activity) co-electrophoresed with 11-S in 6% polyacrylamide gels and co-sedimented with the same form in sucrose density gradients containing 0.1 M NaCl. The purified 11-S enzyme was shown to be homogeneous by sucrose density gradient centrifugation and electrophoresis. These results indicate that 11-S acetylcholinesterase may be unsuitable for some characterization studies due to undetected contamination by the 9.5-S form.
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