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Heparin solubilizes asymmetric acetylcholinesterase from rat neuromuscular junction
Author(s) -
Torres Juan Carlos,
Inestrosa Nibaldo C.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80162-8
Subject(s) - acetylcholinesterase , basal lamina , heparin , neuromuscular junction , glycosaminoglycan , aché , chemistry , heparan sulfate , motor endplate , in vivo , biochemistry , anatomy , enzyme , biophysics , microbiology and biotechnology , biology , neuroscience , ultrastructure
We are interested in the factors involved in the anchorage of acetylcholinesterase (AChE) to the synaptic basal lamina. Here, we report studies showing that heparin, a sulfated glycosaminoglycan, specifically solubilized AChE from endplate regions of rat diaphragm muscle. Of the several molecular forms of AChE present in that region, heparin only released the asymmetric A 12 and A 8 forms of the enzyme. Our results strongly support the involvement of heparin‐like macromolecules in the in vivo immobilization of the collagen‐tailed forms of AChE to the basal lamina of the neuromuscular junction.