Inactive Monomeric Acetyleholinesterase in the Low-Salt-Soluble Extract of the Electric Organ from Torpedo marmorata
Article first published online: 5 OCT 2006
Journal of Neurochemistry
Volume 49, Issue 2, pages 460–467, August 1987
How to Cite
Stieger, S., Brodbeck, U. and Witzemann, V. (1987), Inactive Monomeric Acetyleholinesterase in the Low-Salt-Soluble Extract of the Electric Organ from Torpedo marmorata. Journal of Neurochemistry, 49: 460–467. doi: 10.1111/j.1471-4159.1987.tb02887.x
- Issue published online: 5 OCT 2006
- Article first published online: 5 OCT 2006
- Received June 12, 1986; revised February 5, 1987; accepted February 5,1987.
- Acetylcholinesterase precursor;
- Diisopropylfluorophosphate labelling;
- Proteolytic fragmentation;
- Torpedo marmorata.
Proteolytic fragmentation of (3H]diisopropylflu-orophosphate-labelled catalytic subunits of different molecular forms of acetylcholinesterase demonstrates that all forms extracted from the electric organ from Torpedo marmorata are true acetylcholinesterases. This is supported by immunochemical results showing that the radiolabelled polypeptides are readily recognized by specific anti-acetyl-cholinesterase antibodies. Although distinct structural differences exist, all forms contain a similar peptide carrying the serine hydroxyl of the esteratic subsite. Dimeric, detergent-soluble acetylcholinesterase is present in the low-salt-soluble extract (Mr of the catalytic subunit 66,000) together with a monomeric form (apparent Mr 76,000). This monomeric polypeptide is hydrophilic, enzymatically inactive, and might represent a precursor of the asymmetric forms of acetylcholinesterase.