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Molecular Forms of Acetylcholinesterase: Regulation in a Testosterone‐Sensitive Nerve‐Muscle Axis
Author(s) -
Bleisch William V.,
Luine Victoria N.,
McEwen Bruce S.
Publication year - 1983
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1983.tb08121.x
Subject(s) - acetylcholinesterase , syrinx (medicine) , aché , denervation , zebra finch , castration , endocrinology , medicine , testosterone (patch) , biology , chemistry , anatomy , enzyme , neuroscience , biochemistry , hormone , spinal cord , syringomyelia
We measured the distribution of molecular forms of acetylcholinesterase (AChE) in muscles of a song bird, the zebra finch, and found a pattern similar to those reported in other vertebrates. As in other species, the most rapidly sedimenting form of the enzyme decreases to barely detectable levels following denervation. In the muscles of the syrinx, castration causes a large decrease in AChE activity, but has little or no effect on the relative abundance of AChE forms. This suggests that the number of AChE catalytic sites is changing without affecting the distribution of catalytic sites among the molecular forms. This is in marked contrast with the effect of denervation in the syrinx, which causes changes in the distribution of activity, as well as in total activity.