Summary
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1.
The uptake of γ-aminobutyric acid (GABA) into rat thyroid slices was studied.
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2.
Uptake of 14C-GABA was concentration-dependent: one unsaturable (diffusion) and two saturable components obeying Michaelis-Menten kinetics contributed to transport.
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3.
The kinetic constants of saturable GABA transport systems were: K m1 =1.5 μM, V 1=4.0 nmol×(g wet weight)−1×(20 min)−1 (high-affinity uptake); K m2 =800 μM, V 2=260 nmol×(g wet weight)−1×(20 min)−1 (low-affinity uptake).
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4.
Uptake mediated by each of the carrier systems was concentrative, entirely Na+-dependent, and required activation energies characteristic for active transport.
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5.
High-affinity transport was structurally specific for GABA. The substrate specificity of low-affinity uptake resembled that of β-amino acid transport systems.
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Gebauer, H. GABA transport in the rat thyroid. Naunyn-Schmiedeberg's Arch. Pharmacol. 317, 61–66 (1981). https://doi.org/10.1007/BF00506258
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DOI: https://doi.org/10.1007/BF00506258