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Succinate Dehydrogenase, Monoamine Oxidase and Glutamine Synthetase in Developing Human Foetal Brain Regions
Author(s) -
Mahajan R. G.,
Mandal S.,
Sinha A. K.,
Mukherjee K. L.
Publication year - 1982
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.1471-4159.1982.tb08636.x
Subject(s) - monoamine oxidase , medulla , succinate dehydrogenase , oxidoreductase , glutamine synthetase , medicine , endocrinology , glutamine , biology , monoamine oxidase a , spinal cord , monoamine neurotransmitter , biochemistry , serotonin , enzyme , neuroscience , amino acid , receptor
In human foetal brain ontogeny the cerebral activity of succinate oxidoreductase (EC 1.3.99.1), i.e. succinate dehydrogenase (SDH), is higher than the cerebellar activity. With rise in foetal body weight the activity in all the brain regions gradually declines. SDH in all the brain regions shows two high‐activity periods, one at 20–35 g and another at 110–220 g body weight. The enzyme exhibits a craniocaudal pattern of development. At all times of gestation, l ‐glutamate:ammonia ligase (EC 6.3.1.2), i.e. glutamine synthetase, activity in the spinal cord and medulla is higher than in the other three regions. At 190 g body weight glutamine synthetase shows an activity peak in all brain regions. Monoamine:oxygen oxidoreductase (EC 1.4.3.4), i.e. monoamine oxidase (MAO), is present much before the onset of electrical activity. It develops caudocranially and exhibits a biphasic pattern of development in all the regions. It increases considerably in the medulla and the spinal cord towards late gestational periods.

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