Using selective inhibitor treatments, we have studied the distribution of asymmetric (A) and globular (G) forms of acetylcholinesterase (AChE) in the extra-and intracellular compartments of chick retina, a specialized region of chick central nervous system (CNS). Our results show that the chick retinal collagen-tailed AChE (an example of class I1 asymmetric molecular forms) is essentially an extracellular form of the enzyme; this is the first demonstration of the extracellular localization of asymmetric AChE in the vertebrate CNS. The active site of most of the hydrophobic, membrane-bound G4-form is also exposed to the external environment. In turn, the smaller molecular weight G-forms (G2 and GI) are localized within the cells, where they may represent intermediate components in the assembly or degradation of the more complex enzymatic molecular species.
Histoenzymatic ultrastructural techniques show internal AChE in amacrine as well as in ganglion cell bodies, and external enzyme, specifically associated with synapses and axons, in the inner plexiform layer. The probable cooperation of the extracellular A12forms and the membrane-bound G species (mainly G4) of the enzyme to the hydrolysis of acetylcholine (ACh) released into the external compartment is suggested and discussed.