Solubilization of asymmetric acetylcholinesterase by polyanions.
A number of polyanions, including polysulfates (sulfated glycosaminoglycans (GAGs), dextran and pentosan sulfates, and polyvinylsulfate), polyphosphates (tetrapolyphosphate, polyadenylate) and polycarboxylates (polyaspartate, polyglutamate) solubilize asymmetric acetylcholinesterase (AChE) from chick muscle at low ionic strength, and partially or totally displace AChE tailed forms bound to heparin-agarose columns. The previously reported solubilization of asymmetric AChE by heparin, or the proven affinity of the tailed enzyme forms for this GAG, cannot therefore be taken as direct proof of the involvement of heparin-like heparan sulfate proteoglycans in the anchorage of the collagenous tail of the enzyme to the basal lamina in skeletal muscle.
Centro de Biologia Molecular (CSIC-UAM), Univesidad Autónoma, Madrid, Spain.
J
J
Pérez-Tur
A
A
Barat
M
M
Ramos
G
G
Ramírez
D000110:Acetylcholinesterase / Q000737:chemistry*; D000818:Animals; D000838:Anions / Q000494:pharmacology*; D002645:Chickens; D006025:Glycosaminoglycans / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology; D012995:Solubility
D000838:Anions; D006025:Glycosaminoglycans; D000110:Acetylcholinesterase