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Heparin and the solubilization of asymmetric acetylcholinesterase
Author(s) -
Barat Ana,
Escudero Elena,
Ramírez Galo
Publication year - 1986
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(86)80162-4
Subject(s) - chemistry , heparin , acetylcholinesterase , enzyme , biochemistry , salt (chemistry) , biophysics , extracellular , biology , organic chemistry
Heparin solubilizes asymmetric acetylcholinesterase, from chick skeletal muscle and retina, as a 24 S complex which is quantitatively converted to conventional asymmetric molecular forms of the enzyme (A 12 and A 8 , either class I or class II) upon exposure to high salt. The simultaneous presence of salt and heparin in the homogenization medium selectively prevents, however, the release of class II A‐forms in both muscle and retina. Heparin may generally act by displacing native proteoglycans involved in the attachment of the enzyme tail to the extracellular matrix, or its neural equivalent, being in turn removed by salt to yield typical asymmetric enzyme forms. Heparin would also appear to displace some other molecules specifically involved in the EDTA‐sensitive attachment of class II tailed forms, this effect being antagonized by salt.