A protease is recovered with a dimeric form of acetylcholinesterase in fetal bovine serum.

A protease activity which co-purified with affinity-purified fetal bovine serum acetylcholinesterase (AChE) has been shown to release the amyloid protein precursor (APP) of Alzheimer's disease from cell membranes. The nature of this protease and its relationship to AChE have not been established. In this study, the protease activity was found to be recovered with a minor dimeric form of AChE. This minor form (AChEII) was distinguished from the more abundant tetrameric form (AChEI) by a higher catalytic subunit relative molecular mass (M(r)) of 80,000 (80K), and by a lower affinity for edrophonium-Sepharose. The difference in subunit M(r) was due to differing degrees of glycosylation, as deglycosylation of both AChEI and AChEII gave rise to a similar subunit M(r) of 62K. The protease activity recovered with AChEII was not an intrinsic property of the esterase, as it was separated from the esterase by anion-exchange chromatography, and by immunoprecipitation with anti-AChE antibodies. AChEI possessed a similar subunit M(r) to the tetrameric form of AChE secreted from the bovine adrenal gland, while AChEII possessed a similar subunit molecular weight to the dimeric membrane-bound form of bovine erythrocyte AChE. Thus, it is possible that AChEII may be a solubilised form of a dimeric glycosylphosphatidyl inositol-linked AChE.