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At least 1,063 records · Page 59Linked to original sources
PubMed1986

The induction of mitochondrial L-3-glycerophosphate dehydrogenase by thyroid hormone.

L-3-Glycerophosphate dehydrogenase was purified from porcine brain mitochondria by a shorter and simpler procedure than previously reported. Immunoblotting with antiserum to the porcine enzyme established that rat liver L-3-glycerophosphate dehydrogenase has the same Mr (76 000) by SDS-polyacrylamide gel electrophoresis. In liver mitochondria from normal and hyperthyroid rats, changes in L-3-glycerophosphate dehydrogenase activity were parallelled by changes in enzyme content assayed by immunoblotting. Similar changes were found in the amount of enzyme synthesised in vitro by reticulocyte lysate programmed with rat liver mRNA, suggesting that thyroid hormone causes specific induction of L-3-glycerophosphate dehydrogenase mRNA.

Animals↗
PubMed1977

Effect of dietary DL-ethionine on egg laying and activities of cytoplasmic and mitochondrial L-glycerol 3-phosphate dehydrogenases in liver and kidney of Japanese quail, Coturnix coturnix japonica.

The effect of dietary DL-ethionine on egg laying and activities of succinate dehydrogenases, cytoplasmic and mitochondrial L-glycerol 3-phosphate dehydrogenases, in liver and kidney of Japanese quail, Coturnix coturnix japonica was investigated. When quail at full laying were fed a diet supplemented with DL-ethionine at 0.05%, 0.10%, 0.15% and 0.30% (w/w), respectively, apparent DL-ethionine concentration dependent inhibitions of egg laying rate, weights of ovary and oviduct, and egg weight were observed. At the 0.30% level, activity per g tissue of cytoplasmic L-glygerol 3-phosphate dehydrogenase from liver and kidney decreased to about one-half of the initial activity. A significant difference in the activity of mitochondrial L-glycerol 3-phosphate and succinate dehydrogenase from liver and kidney was obtained between the control and the DL-ethionine fed quail, respectively. These results indicated that dietary DL-ethionine inhibits egg laying and activities of L-glycerol 3-phosphate dehydrogenases and succinate dehydrogenase of both liver and kidney of Japanese quail.

Animals↗
PubMed2005

Upregulation of ALD3 and GPD1 in Saccharomyces cerevisiae during Icewine fermentation.

AIMS: To determine acetic acid, acetaldehyde and glycerol production by wine yeast throughout Icewine fermentation. The expression of yeast cytosolic aldehyde dehydrogenases (ALD3 and ALD6) and glycerol-3-phosphate dehydrogenase (GPD1) were followed to relate metabolites in the wines to expression patterns of these genes. METHODS AND RESULTS: Icewine juice (38.8 degrees Brix, 401 +/- 7 g l(-1) sugar), diluted Icewine juice (21.3 degrees Brix, 211 +/- 7 g l(-1) sugar) and the diluted juice with sugar levels equal to the original Icewine juice (35.6 degrees Brix, 402 +/- 6 g l(-1) sugar) were fermented in triplicate using the commercial wine yeast K1-V1116. Acetic acid production increased 7.1-fold and glycerol production increased 1.8-fold in the Icewine fermentation over that found in the diluted juice fermentation. ALD3 showed a 6.2-fold induction and GPD1 showed a 2.5-fold induction during Icewine vs the diluted fermentation. ALD3 was not glucose repressed when additional sugar was added to diluted juice, but was upregulated 7.0-fold. CONCLUSIONS: The NAD+-dependant aldehyde dehydrogenase encoded by ALD3 appears to contribute to acetic acid production during Icewine fermentation. Expression of GPD1 was upregulated in high sugar fermentations and reflects the elevated levels of glycerol. Solutes in Icewine juice in addition to sugar contribute to the yeast metabolic response. SIGNIFICANCE AND IMPACT OF THE STUDY: This work represents the first descriptive analysis of the fermentation of Canadian Icewine, the expression patterns of yeast genes involved in metabolite production, and their impact on Icewine quality. A role for ALD3 in acetic acid production during Icewine fermentation was found.

Acetaldehyde↗
PubMed1970

Dehydrogenase enzyme cytochemistry of unfixed leucocytes.

An inert, synthetic, sucrose polymer (Ficoll) has been found to have a protective effect on leucocytes during incubation for cytochemical reactions at 37 degrees C. This permits enzyme cytochemistry to be performed on unfixed bone marrow and peripheral blood smears, and on leucocytes cultured in vitro, thus avoiding enzyme inhibition by the use of a fixative. The technique is suitable for the demonstration of both cytoplasmic and intramitochondrial dehydrogenase enzyme activity.

Bone Marrow↗
PubMed1985

[Enzyme activity and content of glycerophosphate shuttle metabolites in the cortex and medulla oblongata during hyperbaric oxygenation therapy of acute hemorrhage].

The experiments on cats have demonstrated that hyperbaric oxygenation (303.9 kPa, 60 min) in acute blood loss (24.0 +/- 0.8 ml/kg) has an essential effect on glycerophosphate shuttle mechanism: it stimulates mitochondrial glycerol-3-phosphate dehydrogenase in the sensorimotor cortex and medulla oblongata, providing glycerol-3-phosphate dehydrogenation, activates cytoplasm hydrogen delivery to mitochondrial respiratory chain, prevents glycerol-3-phosphate and NADH level increase and cytoplasm glycerol-3-phosphate dehydrogenase inhibition, limiting lactate production.

Animals↗
PubMed1977

[Changes in the characteristics of several carbohydrate metabolism enzymes during differentiation of loach skeletal muscle].

The gradual change of enzymes of glycogen metabolism proceeds during the skeletal muscle differentiation in the loach. The portion of the muscle type phosphorylase in the skeletal muscles of the embryo at the stage of the beginning of movement amounts to 30% and that at the stage of hatching to slightly over 50%. At the stage of yolk resorption, the skeletal muscles contain the muscle type phosphorylase only. At the same time the value of KM(UDPG) for glycogen synthetase gradually increases from 0,1 X 10(-3) up to 0,57 X 10(-3) M. The activity of alpha-glycerophosphate dehydrogenase increases more than 70 times.

Animals↗