scholarly journals Substrate specificity of a thymidine phosphorylase in human liver tumor.

1984 ◽  
Vol 32 (5) ◽  
pp. 1919-1921 ◽  
Author(s):  
AKIRA KONO ◽  
YASUHIRO HARA ◽  
SETSURO SUGATA ◽  
YOSHIKAZU MATSUSHIMA ◽  
TOHRU UEDA
Keyword(s):  
Substrate Specificity ◽  
Liver Tumor ◽  
Human Liver ◽  
Thymidine Phosphorylase

scholarly journals Substrate Specificity and Ligand Interactions of CYP26A1, the Human Liver Retinoic Acid Hydroxylase

2011 ◽  
Vol 80 (2) ◽  
pp. 228-239 ◽  
Author(s):  
Jayne E. Thatcher ◽  
Brian Buttrick ◽  
Scott A. Shaffer ◽  
Jakob A. Shimshoni ◽  
David R. Goodlett ◽  
...  
Keyword(s):  
Retinoic Acid ◽  
Substrate Specificity ◽  
Human Liver ◽  
Ligand Interactions

scholarly journals GITR engagement in combination with CTLA-4 blockade completely abrogates immunosuppression mediated by human liver tumor-derived regulatory T cellsex vivo

2015 ◽  
Vol 4 (12) ◽  
pp. e1051297 ◽  
Author(s):  
Alexander Pedroza-Gonzalez ◽  
Guoying Zhou ◽  
Simar Pal Singh ◽  
Patrick PC Boor ◽  
Qiuwei Pan ◽  
...  
Keyword(s):  
Liver Tumor ◽  
Human Liver

Effects of (-)-Menthol on Arylamine N-Acetyltransferase Activity in Human Liver Tumor Cells

2001 ◽  
Vol 29 (02) ◽  
pp. 321-329 ◽  
Author(s):  
Jing-Pin Lin ◽  
Yuh-Ching Li ◽  
Weng-Chuan Lin ◽  
Ching-Liang Hsieh ◽  
Jing-Gung Chung
Keyword(s):  
Tumor Cells ◽  
Liver Tumor ◽  
Human Liver ◽  
High Performance ◽  
Time Course ◽  
Tumor Cell Line ◽  
Intact Cells ◽  
Steady State Kinetic ◽  
Dependent Inhibition ◽  
Dose Dependent Inhibition

To evaluate whether or not (-)-menthol affects arylamine N-acetyltransferase (NAT) activity, we selected human liver tumor cell line (J 5) for examination. By using high performance liquid chromatography, NAT activity for acetylation of 2-aminofluorene (AF) was determined. (-)-Menthol displayed a dose-dependent inhibition to cytosolic NAT activity. Time-course experiments showed that NAT activity measured from intact human liver tumor cells was inhibited by (-)-menthol for up to 24 hrs. But in human liver tumor intact cells, the low doses (0.0032 and 0.032 mM) of (-)-menthol inhibited NAT activity andthe 0.32 mM (-)-menthol did not show any significant differences between control and (-)-menthol treated groups. Using standard steady-state kinetic analysis, it was demonstrated that (-)-menthol was a possible uncompetitive inhibitor (decrease Km and Vmax) to NAT activity in cytosols. This report is the first demonstration which showed (-)-menthol affect on human liver tumor cells NAT activity.

Three-step purification of gp96 from human liver tumor tissues suitable for isolation of gp96-bound peptides

2002 ◽  
Vol 264 (1-2) ◽  
pp. 29-35 ◽  
Author(s):  
Song-Dong Meng ◽  
Jian Song ◽  
Zihe Rao ◽  
Po Tien ◽  
George F. Gao
Keyword(s):  
Liver Tumor ◽  
Human Liver ◽  
Tumor Tissues

ChemInform Abstract: THYMIDINE PHOSPHORYLASE. SUBSTRATE SPECIFICITY FOR 5-SUBSTITUTED 2′-DEOXYURIDINES

1981 ◽  
Vol 12 (5) ◽  
Author(s):  
C. NAKAYAMA ◽  
Y. WATAYA ◽  
R. B. JUN. MEYER ◽  
D. V. SANTI ◽  
M. SANEYOSHI ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Thymidine Phosphorylase

Substrate specificity of Escherichia coli thymidine phosphorylase

2007 ◽  
Vol 72 (1) ◽  
pp. 21-28 ◽  
Author(s):  
N. G. Panova ◽  
C. S. Alexeev ◽  
A. S. Kuzmichov ◽  
E. V. Shcheveleva ◽  
S. A. Gavryushov ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Substrate Specificity ◽  
Thymidine Phosphorylase

scholarly journals Substrate specificity of human liver neutral α-mannosidase

1992 ◽  
Vol 286 (1) ◽  
pp. 47-53 ◽  
Author(s):  
S al Daher ◽  
R De Gasperi ◽  
P Daniel ◽  
S Hirani ◽  
C Warren ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Human Liver ◽  
Core Structure ◽  
Catabolic Pathways ◽  
Mannose Residue ◽  
The Core ◽  
High Mannose

The digestion of radiolabelled natural oligosaccharide substrates by human liver neutral alpha-mannosidase has been studied by h.p.l.c. and h.p.t.l.c. The high-mannose oligosaccharides Man9GlcNAc and Man8GlcNAc are hydrolysed by the enzyme by two distinct non-random routes to a common product of composition Man6GlcNAc, which is then slowly converted into a unique Man5GlcNAc oligosaccharide, Man alpha(1----2)Man alpha(1----2)Man alpha(1----3)[Man alpha (1----6)] Man beta(1----4)GlcNAc. These pathways are different from the processing and lysosomal catabolic pathways for these structures. In particular, the alpha(1----2)-linked mannose residues attached to the core alpha(1----3)-linked mannose residue are resistant to hydrolysis. The key processing intermediate, Man alpha(1----3)[Man alpha(1----6)]Man alpha(1----6)[Man alpha(1----3)] Man beta(1----4)GlcNAc, is not produced in the digestion of high-mannose glycans by the neutral alpha-mannosidase, but it is hydrolysed by the enzyme by a non-random route to Man beta(1----4)GlcNAc via the core structure Man alpha(1----3)[Man alpha(1----6)]Man beta(1----4)GlcNAc. In contrast with its ready hydrolysis by lysosomal alpha-mannosidase, the core alpha(1----3)-mannosidic linkage is quite resistant to hydrolysis by neutral alpha-mannosidase. The precise specificity of neutral alpha-mannosidase towards high-mannose oligosaccharides suggests that it has a role in the modification of such structures in the cytosol.

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