title: Globular and asymmetric acetylcholinesterase in frog muscle basal lamina sheaths.
abstract: After denervation in vivo, the frog cutaneus pectoris muscle can be led to degenerate by sectioning the muscle fibers on both sides of the region rich in motor endplate, leaving, 2 wk later, a muscle bridge containing the basal lamina (BL) sheaths of the muscle fibers (28). This preparation still contains various tissue remnants and some acetylcholine receptor-containing membranes. A further mild extraction by Triton X-100, a nonionic detergent, gives a pure BL sheath preparation, devoid of acetylcholine receptors. At the electron microscope level, this latter preparation is essentially composed of the muscle BL with no attached plasmic membrane and cellular component originating from Schwann cells or macrophages. Acetylcholinesterase is still present in high amounts in this BL sheath preparation. In both preparations, five major molecular forms (18, 14, 11, 6, and 3.5 S) can be identified that have either an asymmetric or a globular character. Their relative amount is found to be very similar in the BL and in the motor endplate-rich region of control muscle. Thus, observations show that all acetylcholinesterase forms can be accumulated in frog muscle BL.
mesh_terms: D000110:Acetylcholinesterase / Q000032:analysis*; D000818:Animals; D001485:Basement Membrane / Q000201:enzymology*; D008297:Male; D009045:Motor Endplate / Q000201:enzymology; D009124:Muscle Proteins / Q000032:analysis*; D011487:Protein Conformation; D011896:Rana temporaria / Q000033:anatomy & histology / Q000378:metabolism
chemical_list: D009124:Muscle Proteins; D000110:Acetylcholinesterase