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Membrane transport of aromatic amino acids by Hymenolepis diminuta (Cestoda)

Published online by Cambridge University Press:  06 April 2009

P. W. Pappas  and
H. R. Gamble
P. W. Pappas
Affiliation:
College of Biological Sciences, Department of Zoology, The Ohio State University, Columbus, Ohio 43210
H. R. Gamble
Affiliation:
College of Biological Sciences, Department of Zoology, The Ohio State University, Columbus, Ohio 43210
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Summary

Aromatic amino acids (phenylalanine, tryptophan and tyrosine) are absorbed by Hymenolepis diminuta through a combination of mediated (non-Na+-sensitive) transport and diffusion. All 3 amino acids are accumulated against an apparent concentration difference during a 30-min incubation of tapeworms in 0·1 mM 3H-labelled amino acid. Inhibitor studies demonstrate that phenylalanine, tryptophan and tyrosine are mutually competitive inhibitors of the uptake of each other, and the uptake of these amino acids is inhibited by aliphatic amino acids but not by basic or dicarboxylic amino acids. The D- and L-isomers of aromatic amino acids are equally effective in inhibiting aromatic amino acid uptake. The data indicate that at least 3 amino acid transport loci are involved in aromatic amino acid transport by H. diminuta.

Type
Research Article
Information
Parasitology , Volume 81 , Issue 2 , October 1980 , pp. 395 - 403
Copyright
Copyright © Cambridge University Press 1980

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