[Biochemical characteristics of membrane fractions from different types of cerebral cortex synaptosomes].
The activity of acetylcholinesterase (ACE) and Na, K-ATPase is distributed among three subfractions of synaptic membranes isolated from light (C) and heavy (D) synaptosomes of the optic area of the rabbit cerebral cortex. The levels of specific activity of both enzymes in C subfractions are similar to those in D subfractions. At the same time the specific activity of ACE and Na, K-ATPase in membrane fractions from both light and heavy synaptosomes is different. Such a biochemistry of subsynaptic components from certain brain structures favors studying a fine morphochemical organization of an isolated nerve terminal and its relationship with the activity of CNS in different functional states.
D000110:Acetylcholinesterase / Q000032:analysis; D000818:Animals; D002540:Cerebral Cortex / Q000032:analysis / Q000201:enzymology / Q000648:ultrastructure*; D007770:L-Lactate Dehydrogenase / Q000032:analysis; D008995:Monoamine Oxidase / Q000032:analysis; D009419:Nerve Tissue Proteins / Q000032:analysis*; D011817:Rabbits; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D013574:Synaptosomes / Q000032:analysis / Q000201:enzymology
D009419:Nerve Tissue Proteins; D007770:L-Lactate Dehydrogenase; D008995:Monoamine Oxidase; D000110:Acetylcholinesterase; D000254:Sodium-Potassium-Exchanging ATPase
Biokhimicheskaia kharakteristika membrannykh fraktsiĭ iz razlichnykh tipov sinaptosom kory bol'shikh polushariĭ.