Does intrapartum antibiotic prophylaxis decrease the incidence of maternal group B streptococcal infections?
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Biomedical subjects
Publications and source records attributed to C Battie.
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Kynurenine-3-hydroxylase, an enzyme that is part of the degradative pathway for tryptophan, was present in the cerebral cortex of neonatal rats and exhibited a Km for L-kynurenine close to that of the liver enzyme. This enzyme was enriched in mitochondrial fractions isolated from cerebral cortices of neonatal rats by Ficoll--sucrose gradient centrifugation, with some activity also present in synaptosomal fractions probably due to the mitochondrial content of synaptosomes since cytochrome c oxidase, another mitochondrial enzyme, had a similar distribution in the gradient. Kynurenine hydroxylase as well as monoamine oxidase, another mitochondrial enzyme, had increased specific activities in synaptosomal fractions isolated from 14-day-old rats compared to fractions from 8-day-old rats. Hypothyroidism, induced on the day of birth, resulted in increased activities of kynurenine hydroxylase and monoamine oxidase in synaptosomal fractions isolated from 14-day-old rats.
The activities of the various molecular forms of acetylcholinesterase (AChE) were measured in monolayer cultures of neonatal rat pineal cells grown alone and in co-culture with sympathetic neurons. AChE forms characterized by sedimentation coefficients of 4S, 6.5S, and 10S were found in he neuronal and pineal cultures, as well as in the co-cultures. The 16S AChE form was found only in the neuronal cultures. Total AChE activity increased with culture age in the co-cultures, but it decreased in pineal cells cultured alone. The low level of activity present in the neuronal cultures did not change markedly over the 27-day culture period. These results, which show bidirectional neuron-pineal cell effects, suggest that AChE molecular forms may be important markers to study the mechanisms underlying neuron-target cell interaction in the developing sympathetic nervous system.
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