Results 161 to 170 of about 9,031 (203)
Acquisition of resistance to antifolates caused by enhanced gamma-glutamyl hydrolase activity.
A subline of H35 hepatoma cells has been developed which exhibits 80-fold resistance to 5,10-dideazatetrahydrofolate, an antifolate which inhibits glycinamideribonucleotide transformylase. The cells are cross-resistant to methotrexate, an inhibitor of dihydrofolate reductase and 10-propargyl-5,8-dideazafolate and its 2-desamino-2-methyl derivative ...
Myung S. Rhee +3 more
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Characterization of human cellular gamma-glutamyl hydrolase.
A previously identified cDNA encoding a human gamma-glutamyl hydrolase was expressed in a baculovirus system. The expressed protein had molecular mass of 37 kDa. Treatment of the protein with PNGase F produced a protein of molecular mass of 30 kDa, indicating that the protein contained asparagine-linked glycosylation. Sequence analysis of the expressed
Myung S. Rhee +4 more
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Although 5-fluorouracil (5-FU) plus leucovorin (LV) is a standard chemotherapy regimen for colorectal cancer, the factors that determine the LV-mediated enhancement of the antitumor activity of 5-FU have remained unknown. We investigated the roles of folylpolyglutamate synthase (FPGS) and gamma-glutamyl hydrolase (GGH), which are the main enzymes ...
Etsuko Sakamoto +10 more
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Secretion of gamma-glutamyl hydrolase in vitro.
Cancer research, 1991gamma-Glutamyl hydrolase (also known as conjugase) is a ubiquitous enzyme that has the capacity to cleave folyl- and antifolylpolyglutamates. This study has revealed that the enzyme is secreted by primary cultures of rat hepatocytes and by H35 hepatoma cells.
B M, O'Connor +4 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
The molecular weight of gamma-glutamyl transferase from normal rat liver and hepatoma tissue was determined by radiation-inactivation and found to be approx 100000 in each case. The molecular weight previously reported for the subunit containing the gamma-glutamyl binding site (22000) is considerably less than that of the holoenzyme, suggesting that in
J L, Ding +3 more
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The molecular weight of gamma-glutamyl transferase from normal rat liver and hepatoma tissue was determined by radiation-inactivation and found to be approx 100000 in each case. The molecular weight previously reported for the subunit containing the gamma-glutamyl binding site (22000) is considerably less than that of the holoenzyme, suggesting that in
J L, Ding +3 more
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Effects of overexpression of gamma-Glutamyl hydrolase on methotrexate metabolism and resistance.
Intracellular metabolism of methotrexate (MTX) to MTX-polyglutamates (MTXPG) is one determinant of cytotoxicity. Steady-state accumulation of MTXPG seems to depend on the activity of two enzymes: folylpolyglutamate synthetase (FPGS), which adds glutamate residues, and gamma-glutamyl hydrolase (GGH), which removes them.
Peter D. Cole +6 more
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Proliferation-dependency of γ-glutamyl hydrolase activity in various mouse cells
Cell Biology International Reports, 1992The activity of gamma-glutamyl hydrolase, the enzyme which deglutamylates folyl and antifolyl polyglutamates, changed significantly in mouse cells during different phases of growth, being about two times lower in actively proliferating mice splenocytes and fibroblasts than in nondividing cells.
E, Sikora +2 more
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A central role for gamma-glutamyl hydrolases in plant folate homeostasis.
The Plant journal : for cell and molecular biology, 2011Most cellular folates carry a short poly-γ-glutamate tail, and this tail is believed to affect their efficacy and stability. The tail can be removed by γ-glutamyl hydrolase (GGH; EC 3.4.19.9), a vacuolar enzyme whose role in folate homeostasis remains unclear.
Tariq A, Akhtar +6 more
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The properties of the secreted γ-glutamyl hydrolases from H35 hepatoma cells
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993gamma-Glutamyl hydrolase has been partially purified and characterized from conditioned culture medium of H35 hepatoma cells. Evidence for heterogeneity of the enzyme is derived from its elution as three distinct peaks of enzymatic activity when the enzyme is purified by TSK-butyl-Sepharose column chromatography.
Y, Wang +4 more
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Properties of Folic Acid γ-Glutamyl Hydrolase (Conjugase) in Rat Bile and Plasma
The Journal of Nutrition, 1981The properties of folic acid gamma-glutamyl hydrolase (conjugase) [EC 3.4.12.10] in rat bile and plasma were investigated. Conjugase activity in bile showed two pH optima; one at pH 4.5-5.0 and one at pH 6.7-7.5. The enzyme activity in plasma had a broad pH--profile with an optimum at pH 6.2-7.5.
D W, Horne, C L, Krumdieck, C, Wagner
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