Muller_1985_Brain.Res_331_295

Reference

Title : Molecular forms and solubility of acetylcholinesterase during the embryonic development of rat and human brain - Muller_1985_Brain.Res_331_295
Author(s) : Muller F , Dumez Y , Massoulie J
Ref : Brain Research , 331 :295 , 1985
Abstract :

Acetylcholinesterase (EC 3.1.1.7) and butyrylcholinesterase (EC 3.1.1.8) form homologous sets of multiple molecular forms. The central nervous system of mammals contains mostly tetramers (G4) and monomers (G1). Their proportions have been shown to vary during maturation in rat brain. In order to examine whether a similar evolution occurs in the human, we performed parallel studies of the activity, solubility and molecular forms of acetylcholinesterase in rat and human brains at various stages. We find both similarities and differences: in rat brain, the enzyme increases mostly postnatally but in human brain acetylcholinesterase reaches a maximum at birth. There is an increase in the proportion of G4 and a decrease in the solubility of this from in the absence of detergent in human as well as in rat brain. These changes occur around birth in rat, but during early pregnancy, before 11 weeks in human brain. In both species, the solubility of the enzyme in detergent-free buffers decreases progressively from more than 50% before birth to about 10-20% in the adult. In addition we analyzed butyrylcholinesterase as well as the levels of the neuron-specific enolase and of the glial S-100 protein. In human, gamma gamma-enolase rises to its adult level after birth, but before the S-100 protein.

PubMedSearch : Muller_1985_Brain.Res_331_295
PubMedID: 3986571

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Citations formats

Muller F, Dumez Y, Massoulie J (1985)
Molecular forms and solubility of acetylcholinesterase during the embryonic development of rat and human brain
Brain Research 331 :295

Muller F, Dumez Y, Massoulie J (1985)
Brain Research 331 :295