The collagen-like subunits of acetylcholinesterase from the eel electrophorus electricus

Abstract

Pepsin-resistant fragments of the tail subunits of 14S and 18S acetylcholinesterase from eel electric organ have been isolated and characterized. The native fragments are composed of three 24,000 molecular weight polypeptides linked by intersubunit disulfide bonds in a collagen-like triple helix. Intact tail subunits have also been isolated. These subunits appear to contain both the triple-helical domain and a noncollagenous domain that is linked to catalytic subunits by disulfide bonds.