Abstract

The effect of heparin, a sulphated glycosaminoglycan, on the solubilization of rat sciatic-nerve acetylcholinesterase (acetylcholine acetylhydrolase; AChE; EC 3.1.1.7) was studied. It was found that heparin solubilized esterase activity from ligated nerves. Sedimentation analysis revealed this activity to be mainly the 16S form. Chondroitin sulphate did not solubilize AChE activity, and protamine eliminated the solubilizing effect. Our results suggest the involvement of sulphated glycosaminoglycans in the intra-axonal localization and transport of 16S AChE.