1887

Abstract

MNF3841 grown on glucose/NHCl constitutively transported -asparagine, -aspartate, -glutamate, -glutamine, glycine, -leucine, -methionine and -phenylalanine. Transport rates were increased 1.5-4-fold by growth on glucose/-glutamate. Uptake of L-glutamate, -glutamine, -asparagine and -leucine was inhibited to varying extents by a broad range of -amino acids. Analogues of -glutamate in which the amino group or -hydrogen was methylated inhibited L-glutamate transport much less effectively. Also while 2-and 3-amino acids interfered with -glutamate uptake, -glutamate did not. Inhibition by 2,4-dinitrophenol, carbonyl cyanide -chlorophenylhydrazone and cyanide indicated that amino acid transport was active. The ratio of the intracellular to extracellular concentration of -leucine after 5 min accumulation was 768. Cells loaded with -[C]leucine exhibited exchange not only with external -leucine but also with -glutamate. The apparent for -glutamate transport was 0·081 μ. Both -aspartate and -alanine were competitive inhibitors of -glutamate uptake with apparent values of 0·164 μ and 2·3 μ, respectively. These results suggest that there is an extremely high affinity carrier for -glutamate that is not only very sensitive to inhibition by -aspartate but also capable of being inhibited by a broad range of amino acids at an order of magnitude higher concentration.

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1985-06-01
2022-01-29
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