Barat A, Escudero E, Ramírez G
FEBS Lett. 1986 Jan 20;195(1-2):209-14. doi: 10.1016/0014-5793(86)80162-4.
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 (A12 and A8, 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.
肝素可溶解来自鸡骨骼肌和视网膜的不对称乙酰胆碱酯酶，形成一种24 S复合物，该复合物在暴露于高盐时会定量转化为该酶的传统不对称分子形式（A12和A8，I类或II类）。然而，在匀浆介质中同时存在盐和肝素时，会选择性地阻止肌肉和视网膜中II类A形式的释放。肝素通常可能通过取代参与酶尾部附着于细胞外基质或其神经等效物的天然蛋白聚糖起作用，而这些蛋白聚糖又会被盐去除，从而产生典型的不对称酶形式。肝素似乎还会取代一些其他专门参与II类尾部形式的EDTA敏感附着的分子，这种作用会被盐拮抗。
