Major component of acetylcholinesterase in Torpedo electroplax is not basal lamina associated

Abstract

Electroplax tissue from Torpedo californica contains two major structural forms of the enzyme acetylcholinesterase. One form, composed of tetrameric protomers which are further aggregated by interactions among associated collagenous "tail fibers", has been well characterized previously. This form is associated in situ with the basal lamina. The other form is described and characterized herein. This latter form accounts for at least 50% of the acetylcholinesterase activity of the tissue. This enzyme associated with the tissue phospholipids. It aggregates in aqueous solution but readily dissociates to dimers in 1% sodium cholate solution, a solvent in which it is both soluble and catalytically fully active. The same dimer is obtained in sodium dodecyl sulfate solution where the enzyme is denatured. Denaturation in the presence of the reductant dithiothreitol results in the formation of a single 80000-dalton subunit. The purified enzyme contains no collagenous component. It is not derivable from the collagenous "tailed-enzyme" form in the tissue homogenate. However, the two enzymes have similar molecular weight catalytic subunits and the same substrate-dependent turnover numbers (per active site) for a variety of choline esters which are generally utilized to distinguish specific esterase function. In the tissue homogenate each form of the enzyme is associated with a characteristic structural component (phospholipid or collagen). By implication, acetylcholinesterase function is localized in situ in the phospholipid membrane as well as at the basal lamina.