Isoenzyme pattern of malate dehydrogenase during respiratory derepression in Schizosaccharomyces pombe

Flury, Urs; Heer, Beat; Fiechter, Armin

doi:10.1007/bf00403053

Cited by 10 publications

(6 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Such a mechanism was discussed by Flury et al [55] for the yeast Schizosaccharomyces pombe. It seemed reliable also for Saccharomyces cerevisiae, because in this yeast the extend of derepression is always proportional to the amount of mitochondrial malate dehydrogenase which is present before derepression.…”

Section: Discussionmentioning

confidence: 94%

The Malate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae. Purification, Characterisation and Studies on Their Regulation

1978

View full text Add to dashboard Cite

1. One mitochondrial and one cytoplasmic malate dehydrogenase isoenzyme could be purified from acetate grown cells of the yeast Saccharomyces cerevisiae. 2. The purification procedure uses chromatography on dextran blue columns as an essential step for enrichment, and reverse ammonium sulfate chromatography on celite for isoenzyme separation. 3. The homogeneity of the preparations was established by gel electrophoreses in the presence of sodium dodecylsulfate and by a sedimentation run in the analytical ultracentrifuge. 4. Both enzymes are dimers with a molecular weight of 75 000 for the cytoplasmic and of 68 000 for the mitochondrial enzyme. 5. Amino acid analysis and peptide mapping showed that both enzymes are closely related, but genetically different (true isoenzymes). 6. The cytoplasmic enzyme shows electrophoretic splitting. This is most likely due to post‐translational deamination in vivo. 7. Antibodies to both isoenzymes could be obtained in rabbits. The antisera to cytoplasmic malate dehydrogenase were specific for this enzyme. Antisera to mitochondrial malate dehydrogenase react with both isoenzymes. Neither type of antisera precipitated an inactive protein after the glucose‐dependent inactivation of cytoplasmic malate dehydrogenase in vivo.

show abstract

Section: Discussionmentioning

confidence: 94%

The Malate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae. Purification, Characterisation and Studies on Their Regulation

1978

View full text Add to dashboard Cite

show abstract

“…Isoelectric focusing. Isoelectric focusing was performed at 40C for 5 h in cylindrical polyacrylamide gels (0.6 by 9 cm) containing 5% acrylamide, 6 M urea, and 0.2% Ampholine (pH 3 to 10). Immunoprecipitates were solubilized by incubation with 6 M urea and 25 mM dithiothreitol for 30 min at 950C, after which the samples were made 2.5% (vol/vol) with ampholyte and 10% (wt/vol) with sucrose.…”

Section: Rapid Inactivation Of Glutamate Dehydrogenasementioning

confidence: 99%

Evidence for the Degradation of Nicotinamide Adenine Dinucleotide Phosphate-Dependent Glutamate Dehydrogenase of Candida utilis During Rapid Enzyme Inactivation

Hemmings

1978

J Bacteriol

View full text Add to dashboard Cite

The nicotinamide adenine dinucleotide phosphate-dependent glutamate dehydrogenase (NADP-GDH) from the food yeast Candida utilis was found to be rapidly inactivated when cultures were starved of a carbon source. The addition of glutamate or alanine to the starvation medium stimulated the rate of inactivation. Loss of enzyme activity was irreversible since the reappearance of enzyme activity, following the addition of glucose to carbon-starved cultures, was blocked by cycloheximide. A specific rabbit antibody was prepared against the NADP-GDH from C. utilis and used to quantitate the enzyme during inactivation promoted by carbon starvation. The amount of precipitable antigenic material paralleled the rapid decrease of enzyme activity observed after transition of cells from NH 4 + -glucose to glutamate medium. No additional small-molecular-weight protein was precipitated by the antibody as a result of the inactivation, suggesting that the enzyme is considerably altered during the primary steps of the inactivation process. Analysis by immunoprecipitation of the reappearance of enzyme activity after enzyme inactivation showed that increase of NADP-GDH activity was almost totally due to de novo synthesis, ruling out the possibility that enzyme activity modulation is achieved by reversible covalent modification. Enzyme degradation was also measured during steady-state growth and other changes in nitrogen and carbon status of the culture media. In all instances so far estimated, the enzyme was found to be very stable and not normally subject to high rates of degradation. Therefore, the possibility that inactivation was caused by a change in the ratio of synthesis to degradation can be excluded.

show abstract

“…2A). The reason for this is the fact that in contrast to S. cerevisiae, S. pombe oxidizes ethanol to CO 2 and H 2 O mainly for energetic purposes (14,20 …”

Section: Resultsmentioning

confidence: 99%

Effect of Cd²⁺on the Antioxidant Status ofShizosaccharomyces Pombe

Pisareva

Kostova

Nedeva

et al. 2010

Biotechnology & Biotechnological Equipment

View full text Add to dashboard Cite

show abstract

Isoenzyme pattern of malate dehydrogenase during respiratory derepression in Schizosaccharomyces pombe

Cited by 10 publications

References 12 publications

The Malate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae. Purification, Characterisation and Studies on Their Regulation

The Malate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae. Purification, Characterisation and Studies on Their Regulation

Evidence for the Degradation of Nicotinamide Adenine Dinucleotide Phosphate-Dependent Glutamate Dehydrogenase of Candida utilis During Rapid Enzyme Inactivation

Effect of Cd²⁺on the Antioxidant Status ofShizosaccharomyces Pombe

Contact Info

Product

Resources

About

Isoenzyme pattern of malate dehydrogenase during respiratory derepression in Schizosaccharomyces pombe

Cited by 10 publications

References 12 publications

The Malate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae. Purification, Characterisation and Studies on Their Regulation

The Malate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae. Purification, Characterisation and Studies on Their Regulation

Evidence for the Degradation of Nicotinamide Adenine Dinucleotide Phosphate-Dependent Glutamate Dehydrogenase of Candida utilis During Rapid Enzyme Inactivation

Effect of Cd2+on the Antioxidant Status ofShizosaccharomyces Pombe

Contact Info

Product

Resources

About

Effect of Cd²⁺on the Antioxidant Status ofShizosaccharomyces Pombe