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The inhibition by 6‐diazo‐5‐oxo‐L‐norleucine of glutamine catabolism of the cultured human lymphoblast
Author(s) -
Willis Randall C.,
Edwin Seegmiller J.
Publication year - 1977
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1040930308
Subject(s) - glutamine , lymphoblast , norleucine , incubation , catabolism , biochemistry , cell culture , azaserine , microbiology and biotechnology , biology , glutaminase , chemistry , metabolism , amino acid , methionine , genetics
The rapid catabolism of glutamine by the cultured human lymphoblast line WI‐L2 can be inhibited greater than 95% by incubation of cell suspensions with 6‐diazo‐5‐oxo‐L‐norleucine (DON). The inhibition persists for at least four hours after removal of DON from the cell suspension. The exposure of cells to DON inhibits over 95% of the glutaminase activity measured in lysates in the presence of either phosphate or maleate. Similarly, γ‐glutamyl transpeptidase, assayed with γ‐glutamyl‐p‐nitroanilide as substrate and glycylglycine as acceptor, is inhibited over 90%. DON‐treated and control cells accumulated radioactive material from suspensions containing [ 14 C]‐L‐glutamine at similar initial rates; the radioactive material accumulated by the DON‐treated cells is all recoverable as glutamine while the radioactive material accumulated by untreated cells is principally recovered as glutamate.