Journal of Bioenergetics and Biomembranes

, Volume 23, Issue 4, pp 689–697 | Cite as

l-Glutamine transport in native vesicles isolated from Ehrlich ascites tumor cell membranes

  • Miguel A. Medina
  • Ana R. Quesada
  • Ignacio Núñez de Castro
Research Articles

Abstract

Native vesicles isolated from Ehrlich ascites tumor cells accumulate glutamine by means of Na+-dependent transport systems; thiocyanate seems to be the more effective anion. The apparent affinity constant for the process was 0.38 mM. The Arrhenius plot gave an apparent activation energy of 12.3 kJ/mol. The structural analogs of glutamine, acivicin (2.5 mM) and azaserine (2.5 mM), inhibited the net uptake by 67 and 70%, respectively. The sulfhydryl reagents mersalyl, PCMBS, NEM, and DTNB also inhibited net uptake, suggesting that sulfhydryl groups may be involved in the activity of the carrier protein. A strong inhibition was detected when the vesicles were incubated in the presence of alanine, cysteine, or serine; in addition, histidine, but not glutamate or leucine, had a negative effect on glutamine transport.

Key Words

l-Glutamine amino acid transport plasma membrane vesicle Ehrlich cells 

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Copyright information

© Plenum Publishing Corporation 1991

Authors and Affiliations

  • Miguel A. Medina
    • 1
  • Ana R. Quesada
    • 1
    • 2
  • Ignacio Núñez de Castro
    • 1
  1. 1.Laboratorio de Bioquímica y Biología Molecular, Facultad de CienciasUniversidad de MálagaMálagaSpain
  2. 2.Antibióticos FarmaMadridSpain

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