hexacyanoferrate-iii and Carcinoma--Ehrlich-Tumor

hexacyanoferrate-iii has been researched along with Carcinoma--Ehrlich-Tumor* in 2 studies

Other Studies

2 other study(ies) available for hexacyanoferrate-iii and Carcinoma--Ehrlich-Tumor

Article	Year
Putrescine and chlorpheniramine inhibit Ehrlich ascites tumor cell plasma membrane ferricyanide reductase activity. Cancer letters, 1998, Oct-23, Volume: 132, Issue:1-2 The presence of putrescine or chlorpheniramine in the incubation medium of Ehrlich ascites tumor cells starved for 1 h significantly inhibits the rate of ferricyanide reduction by their plasma membrane redox system. Freshly harvested cells, without depletion of their intracellular pools of polyamines, and cells preincubated under conditions arranged to increase ornithine decarboxylase activity also reduced externally added ferricyanide at a lower rate than those cells starved for 1 h. All these data seems to indicate that the presence of putrescine is enough to significantly inhibit Ehrlich cell plasma membrane redox system activity. Topics: Animals; Carcinoma, Ehrlich Tumor; Cell Membrane; Chlorpheniramine; Female; Ferricyanides; Histamine H1 Antagonists; Kinetics; Mice; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Putrescine; Tumor Cells, Cultured	1998
Purification and characterization of a plasma membrane ferricyanide-utilizing NADH dehydrogenase from Ehrlich tumour cells. The Biochemical journal, 1996, Mar-01, Volume: 314 ( Pt 2) A ferricyanide-utilizing NADH dehydrogenase (NADH-ferricyanide oxidoreductase) from the plasma membrane of Ehrlich ascites tumour cells has been purified about 1500-fold to apparent homogeneity. The method comprises the isolation of an enriched plasma membrane fraction, solubilization with Triton X-100, ion-exchange chromatography, ammonium sulphate precipitation, Cibacron Blue chromatography and fast-protein liquid chromatography with a Superose-6 gel filtration column. The specific activity of the final pool was more than 61 units/mg protein. The pure enzyme examined by SDS/PAGE displayed only one type of subunit with an apparent molecular mass of 32.0 kDa. The molecular mass of the native protein (117.0 kDa) was estimated by gel filtration; these results suggest a protein composed of four subunits of identical molecular mass. The enzyme was stable in the pH interval between 6 and 9, with maximum activity at pH values from 7.5 to 8.5. The purified enzyme showed Michaelis-Menten kinetics for the substrates, with apparent K(m) values of 4.3 X 10(-5) M and 6.7 X 10(-5) M for NADH and ferricyanide respectively. The isolated protein was strongly inhibited by Zn2+ and the thio-specific reagents mersalyl and p-chloromercuribenzenesulphonic acid. Topics: Animals; Carcinoma, Ehrlich Tumor; Cell Membrane; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Female; Ferricyanides; Hydrogen-Ion Concentration; Kinetics; Mice; Molecular Weight; NADH Dehydrogenase; Solubility	1996

Article

Year

Putrescine and chlorpheniramine inhibit Ehrlich ascites tumor cell plasma membrane ferricyanide reductase activity.

Cancer letters, 1998, Oct-23, Volume: 132, Issue:1-2

The presence of putrescine or chlorpheniramine in the incubation medium of Ehrlich ascites tumor cells starved for 1 h significantly inhibits the rate of ferricyanide reduction by their plasma membrane redox system. Freshly harvested cells, without depletion of their intracellular pools of polyamines, and cells preincubated under conditions arranged to increase ornithine decarboxylase activity also reduced externally added ferricyanide at a lower rate than those cells starved for 1 h. All these data seems to indicate that the presence of putrescine is enough to significantly inhibit Ehrlich cell plasma membrane redox system activity.

Topics: Animals; Carcinoma, Ehrlich Tumor; Cell Membrane; Chlorpheniramine; Female; Ferricyanides; Histamine H1 Antagonists; Kinetics; Mice; NADH, NADPH Oxidoreductases; Oxidation-Reduction; Putrescine; Tumor Cells, Cultured

1998

Purification and characterization of a plasma membrane ferricyanide-utilizing NADH dehydrogenase from Ehrlich tumour cells.

The Biochemical journal, 1996, Mar-01, Volume: 314 ( Pt 2)

A ferricyanide-utilizing NADH dehydrogenase (NADH-ferricyanide oxidoreductase) from the plasma membrane of Ehrlich ascites tumour cells has been purified about 1500-fold to apparent homogeneity. The method comprises the isolation of an enriched plasma membrane fraction, solubilization with Triton X-100, ion-exchange chromatography, ammonium sulphate precipitation, Cibacron Blue chromatography and fast-protein liquid chromatography with a Superose-6 gel filtration column. The specific activity of the final pool was more than 61 units/mg protein. The pure enzyme examined by SDS/PAGE displayed only one type of subunit with an apparent molecular mass of 32.0 kDa. The molecular mass of the native protein (117.0 kDa) was estimated by gel filtration; these results suggest a protein composed of four subunits of identical molecular mass. The enzyme was stable in the pH interval between 6 and 9, with maximum activity at pH values from 7.5 to 8.5. The purified enzyme showed Michaelis-Menten kinetics for the substrates, with apparent K(m) values of 4.3 X 10(-5) M and 6.7 X 10(-5) M for NADH and ferricyanide respectively. The isolated protein was strongly inhibited by Zn2+ and the thio-specific reagents mersalyl and p-chloromercuribenzenesulphonic acid.

Topics: Animals; Carcinoma, Ehrlich Tumor; Cell Membrane; Chromatography, Affinity; Electrophoresis, Polyacrylamide Gel; Female; Ferricyanides; Hydrogen-Ion Concentration; Kinetics; Mice; Molecular Weight; NADH Dehydrogenase; Solubility

1996