Choline acetyltransferase activities in single motor neurons from vertebrate spinal cords.

Single cell bodies of spinal motor neurons were isolated from freeze-dried sections of fresh spinal cords from six species of vertebrates. Single human neurons were also isolated from the spinal cords of three autopsy cases without neurological diseases. Choline acetyltransferase activity of these single neurons was determined by measuring acetyl-CoA formation from CoASH and acetylcholine by use of the enzymatic amplification reactions, CoA and NADP cyclings. The enzyme activity was unevenly distributed in the cytosol of spinal motor neurons of all species, but not measurable in rabbit dorsal root ganglion cells. The specific activity on a dry weight basis varied widely among the individual neurons from the species studied. The average activity was highest with rat neurons and lowest with yellowtail neurons. The neurons from cold-blooded animals (bullfrog and yellowtail) had about one-tenth the activity compared with the warm-blooded animals (cat, rabbit, rat, and hen). Human neurons, obtained under different morbid and post-mortem conditions with three autopsy cases, had very low activities corresponding to those of cold-blooded animals. Since the choline acetyltransferase activity lost from mouse brain after 11 h at 38 degrees C was 50%, the activity in human neurons was believed to actually be low in vivo.