Inactive monomeric acetylcholinesterase in the low-salt-soluble extract of the electric organ from Torpedo marmorata.

Abstract:

:Proteolytic fragmentation of [3H]diisopropylfluorophosphate-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-acetylcholinesterase 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.

journal_name

J Neurochem

authors

Stieger S,Brodbeck U,Witzemann V

doi

10.1111/j.1471-4159.1987.tb02887.x

subject

Has Abstract

pub_date

1987-08-01 00:00:00

pages

460-7

issue

2

eissn

0022-3042

issn

1471-4159

journal_volume

49

pub_type

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