Uptake and utilization of L-glutamine by human lymphoid cells; relationship to γ-glutamyl transpeptidase activity Academic Article Article uri icon


MeSH Major

  • Carrier Proteins
  • Cell Membrane
  • Endoplasmic Reticulum
  • Mitochondrial Proteins
  • Saccharomyces cerevisiae Proteins
  • Sterols


  • Initial rates of glutamine uptake were studied in human lymphoid cell lines whose γ-glutamyl transpeptidase activities vary from 93 to 11,300 units/mg. In general, glutamine was transported at lower rates than other amino acids (met, phe, leu) in all cell lines studied. A cell line with very high transpeptidase activity exhibited an increased rate of glutamine uptake as compared to other amino acids, and a markedly decreased intracellular concentration of glutamine. In all cell lines transported glutamine was extensively (80%) converted to glutamate. Treatment of cells with 6-diazo-5-oxo-L-norleucine (DON) decreased transpeptidase and conversion of transported glutamine to glutamate by about 80%. Inhibition of glutamine transport was less pronounced (0-20%). The findings indicate that transported glutamine does not equilibrate with glutamine in the intracellular pool, but may enter a separate pool in which it is rapidly converted to glutamate. © 1977.

publication date

  • September 9, 1977



  • Academic Article


Digital Object Identifier (DOI)

  • 10.1016/0006-291X(77)91243-8

PubMed ID

  • 20881

Additional Document Info

start page

  • 222

end page

  • 9


  • 78


  • 1