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PubMed1996

Identification of mRNAs differentially expressed in quiescence or in late G1 phase of the cell cycle in human breast cancer cells by using the differential display method.

BACKGROUND: The decision for a cell to enter the DNA synthesis (S) phase of the cell cycle or to arrest in quiescence is likely to be determined by genes expressed in the late G1 phase, at the restriction point. Loss of restriction point control is associated with malignant cellular transformation and cancer. For this reason, identifying genes that are differentially expressed in late G1 phase versus quiescence is important for understanding the molecular basis of normal and malignant growth. MATERIALS AND METHODS: The differential display (DD) method detects mRNA species that are different between sets of mammalian cells, allowing their recovery and cloning of the corresponding cDNAs. Using this technique, we compared mRNAs from synchronized human breast cancer cells (21 PT) in quiescence and in late G1. RESULTS: Six mRNAs differentially expressed in late G1 or in quiescence were identified. One mRNA expressed 10 hr after serum induction showed 99% homology to a peptide transporter involved in antigen presentation of the class I major histocompatibility complex (TAP-1) mRNA. Another mRNA expressed specifically in quiescence and down-regulated 2 hr following serum induction showed 98% homology to human NADP+ -dependent cytoplasmic malic enzyme (EC1.1.1.40) mRNA, which is an important enzyme in fatty acid synthesis and lipogenesis. Three others showed high homology to different mRNAs in the GeneBank, corresponding to genes having unknown functions. Finally, one mRNA revealed no significant homology to known genes in the GeneBank. CONCLUSIONS: We conclude that DD is an efficient and powerful method for the identification of growth-related genes which may have a role in cancer development.

Base Sequence↗
PubMedDate not supplied

Relation between dietary lipid level and voluntary feed intake, growth, nutrient gain, lipid deposition and hepatic lipogenesis in rainbow trout.

Four diets with differing lipid contents (15, 20, 25 or 30% DM) were tested on small (initial body weight: 27 g) and larger (IBW: 93 g) rainbow trout (Oncorhynchus mykiss) fed on demand or by hand, respectively. In both trials, voluntary feed intake was inversely related to dietary lipid levels. Protein efficiency increased when dietary fat content increased. Final whole-body lipid content was positively related to dietary lipid levels. The main sites of lipid storage were visceral adipose tissue and to a lesser extent muscle. Increased fat deposition in the visceral cavity of young trout was due to both hyperplasic and hypertrophic responses and in larger trout mostly due to a hypertrophic response. Liver activities of glucose-6-phosphate dehydrogenase and fatty acid synthetase were negatively correlated with fat intake and positively with starch intake, whereas malic enzyme was little affected by dietary treatments.

Adipose Tissue↗
PubMed2002

Seasonal variation in carbohydrate and lipid metabolism of yellow perch (Perca flavescens) chronically exposed to metals in the field.

The effects of heavy metals on growth, intermediary metabolism and enzyme activities were investigated in yellow perch (Perca flavescens), sampled in summer and fall from lakes situated along a contamination gradient of Cd, Zn and Cu in the mining region of Rouyn-Noranda, Québec. An exposure-dependent decrease in condition factor was observed in both seasons. Liver glycogen and triglyceride reserves were higher in summer than in fall in fish from the reference lake, while the seasonal pattern was different in fish from the contaminated lakes. Plasma free fatty acids (FFA) levels were also influenced by season and contamination. Activities of malic enzyme (ME) and glucose 6-phosphate dehydrogenase (G6PDH) in the liver were higher in the summer than in the fall in reference lakes whereas no seasonal variations were detected in fish from contaminated lakes. Activities of pyruvate kinase (PyK), aspartate transaminase (AST), phosphoenolpyruvate carboxykinase (PEPCK) and malate dehydrogenase (MDH), were higher in fish from contaminated lakes in fall but not in summer. Chronic exposure of yellow perch to sublethal levels of heavy metals impairs growth and alters the seasonal cycling of liver glycogen and triglycerides as well as the activities of metabolic enzymes.

Animals↗
PubMed2005

Dietary whey protein downregulates fatty acid synthesis in the liver, but upregulates it in skeletal muscle of exercise-trained rats.

OBJECTIVE: This study compared the effects of casein and whey protein as the source of dietary protein on the activity of lipogenic enzymes and mRNA levels in the liver and skeletal muscle of exercise-trained rats. METHODS: Twenty-eight male Sprague-Dawley rats were randomly assigned to one of four groups (n = 7/group). Rats were assigned to sedentary or exercise-trained groups and were fed the casein or whey protein diet. Rats in the exercise groups were trained for 2 wk using a swimming exercise for 120 min/d and 6 d/wk. RESULTS: A significant decrease in the activity of the hepatic lipogenic enzymes, glucose-6-phosphate dehydrogenase, malic enzyme, adenosine triphosphate citrate lyase, acetyl-coenzyme A carboxylase, and fatty acid synthase (FASN) was observed in rats fed whey protein compared with animals fed casein. Compared with the casein diet, the whey protein diet also lowered mRNA expression of these enzymes, except for FASN. In contrast to the findings in liver, whey protein, as compared with casein, increased skeletal muscle FASN activity and mRNA. Further, exercise training resulted in increased skeletal muscle glucose-6-phosphate dehydrogenase and FASN activity and adenosine triphosphate citrate lyase, acetyl-coenzyme A carboxylase-1, and FASN mRNA expression. CONCLUSIONS: Exercise training or whey protein may play an important role in suppressing hepatic fatty acid synthesis, thereby decreasing accumulation of body fat and stimulating the skeletal muscle to increase energy substrate as fat during prolonged exercise.

Analysis of Variance↗
PubMed2006

Lipid lowering effect of S-methyl cysteine sulfoxide from Allium cepa Linn in high cholesterol diet fed rats.

The lipid lowering action of S-methyl cysteine sulfoxide (SMCS) isolated from Allium cepa Linn (family: Liliaceae) was investigated in Sprague-Dawley rats fed on 1% cholesterol diet, in comparison to the hypolipidemic drug gugulipid. Administration of SMCS at a dose of 200mg/kg body weight for 45 days ameliorated the hyperlipidemic condition. The lipid profile in serum and tissues showed that concentrations of cholesterol, triglyceride and phospholipids were significantly reduced when compared to their untreated counterparts. The total lipoprotein lipase activity in the adipose tissue was decreased with also a decrease in the free fatty acid levels in serum and tissues. The activities of the lipogenic enzymes glucose 6-phosphate dehydrogenase and malic enzyme as also of HMG CoA reductase in the tissues remained low on treatment indicating that both the drugs did not favor lipogenesis and cholesterogenesis in the hyperlipidemic animals. The fecal excretion of bile acids and sterols was further increased upon treatment with the drugs. The results are directive to that both gugulipid and SMCS cause reduction of endogenous lipogenesis, increase catabolism of lipids and subsequent excretion of metabolic by-products through the intestinal tract. However, gugulipid is a better drug than SMCS at a low dose of 50mg/kg body weight.

Animals↗
PubMed1994

[Effects of dietary linoleic acid on lipogenesis enzyme activity in adipose tissue in the pig].

The effect of dietary linoleic acid on lipogenesis was determined on 36 Large White castrated male pigs fed between 35 and 100 kg liveweight diets containing 4% of total lipids including 3 levels of linoleic acid 1.5, 2.0 and 2.5%. The elevation in dietary linoleic acid increases the carcass fatness (P < 0.01). At slaughter, linoleic acid content in the backfat increases with the level of dietary linoleic acid (P < 0.001). The lipogenesis measured by the activities of acetyl-coenzyme A carboxylase, malic enzyme and glucose-6-phosphate dehydrogenase increases significantly in adipose tissues (backfat and lean fat) with the dietary linoleic supply, whereas no effect was noticed in intramuscular fat. The increase in fat synthesis can explain the higher increase in carcass fatness of pigs fed diets containing high levels of linoleic acid.

Acetyl-CoA Carboxylase↗
PubMed1996

Purification and characterization of a malic enzyme from the ruminal bacterium Streptococcus bovis ATCC 15352 and cloning and sequencing of its gene.

Malic enzyme (EC 1.1.1.39), which catalyzes L-malate oxidative decarboxylation and pyruvate reductive carboxylation, was purified to homogeneity from Streptococcus bovis ATCC 15352, and properties of this enzyme were determined. The 2.9-kb fragment containing the malic enzyme gene was cloned, and the sequence was determined and analyzed. The enzymatic properties of the S. bovis malic enzyme were almost identical to those of other malic enzymes previously reported. However, we found that the S. bovis malic enzyme catalyzed unknown enzymatic reactions, including reduction of 2-oxoisovalerate, reduction of 2-oxoisocaproate, oxidation of D-2-hydroxyisovalerate, and oxidation of D-2-hydroxyisocaproate. The requirement for cations and the optimum pH of these unique activities were different from the requirement for cations and the optimum pH of the L-malate oxidative decarboxylating activity. A sequence analysis of the cloned fragment revealed the presence of two open reading frames that were 1,299 and 1,170 nucleotides long. The 389-amino-acid polypeptide deduced from the 1,170-nucleotide open reading frame was identified as the malic enzyme; this enzyme exhibited high levels of similarity to malic enzymes of Bacillus stearothermophilus and Haemophilus influenzae and was also similar to other malic enzymes and the malolactic enzyme of Lactococcus lactis.

Amino Acid Sequence↗
PubMed2002

Aspartate aminotransferase isotope exchange reactions: implications for glutamate/glutamine shuttle hypothesis.

Aspartate aminotransferase (AAT) catalyzes amino group transfer from glutamate (Glu) or aspartate (Asp) to a keto acid acceptor-oxaloacetate (OA) or alpha-ketoglutarate (KG), respectively. Data presented here show that AAT catalyzes two partial reactions resulting in isotope exchange between 3H-labeled Glu or 3H-labeled Asp and the cognate keto acid in the absence of the keto acid acceptor required for the net reaction. Tritiated keto acid product was detected by release of 3H2O from C-3 during base-induced enolization. Tritium released directly from C-2 (or C-3) by the enzyme was also evaluated and is a small fraction of that released because of exchange to the keto acid pool. Exchange is dependent on AAT concentration, time-dependent, proportional to the amino-to-keto acid ratio, and blocked by aminooxyacetate (AOA), an AAT inhibitor. Enzymatic conversion of [3H]KG to Glu by glutamic dehydrogenase (GDH) or of [3H]OA to malate by malic dehydrogenase (MDH) "protects" the label from release by base, showing that base-induced isotope release is from keto acid rather than a result of release during the exchange process. AAT isotope exchange is discussed in the context of the glutamate/glutamine shuttle hypothesis for astrocyte/neuron carbon cycling.

Alkalies↗
PubMed2002

Demonstration of pyruvate recycling in primary cultures of neocortical astrocytes but not in neurons.

Pyruvate recycling was studied in primary cultures of mouse cerebrocortical astrocytes, GABAergic cerebrocortical interneurons, and co-cultures consisting of both cell types by measuring production of [4-(13)C]glutamate from [3-(13)C]glutamate by aid of nuclear magnetic resonance spectroscopy. This change in the position of the label can only occur by entry of [3-(13)C]glutamate into the tricarboxylic acid (TCA) cycle, conversion of labeled alpha-ketoglutarate to malate or oxaloacetate, malic enzyme-mediated decarboxylation of malate to pyruvate or phosphoenolpyruvate carboxykinase-mediated conversion of oxaloacetate to phosphoenolpyruvate and subsequent hydrolysis of the latter to pyruvate, and introduction of the labeled pyruvate into the TCA cycle, i.e., after exit of the carbon skeleton of pyruvate from the TCA cycle followed by re-entry of the same pyruvate molecules via acetyl CoA. In agreement with earlier observations, pyruvate recycling was demonstrated in astrocytes, indicating the ability of these cells to undertake complete oxidative degradation of glutamate. The recycled [4-(13)C]glutamate was not further converted to glutamine, showing compartmentation of astrocytic metabolism. Thus, absence of recycling into glutamine in the brain in vivo cannot be taken as indication that pyruvate recycling is absent in astrocytes. No recycling could be demonstrated in the cerebrocortical neurons. This is consistent with a previously demonstrated lack of incorporation of label from glutamate into lactate, and it also indicates that mitochondrial malic enzyme is not operational. Nor was there any indication of pyruvate recycling in the co-cultures. Although this may partly be due to more rapid depletion of glutamate in the co-cultures, this observation at the very least indicates that pyruvate recycling is not up-regulated in the neuronal-astrocytic co-cultures.

Animals↗
PubMed1985

Comparative changes in the lipogenic enzyme activities and in the in vivo fatty acid synthesis in liver and adipose tissues during the post-weaning growth of male rats.

Changes in the specific activities of acetyl-CoA-carboxylase (ACX), malic enzyme (ME) and glucose-6-phosphate dehydrogenase (G-6-PD) were compared to changes in de novo lipogenesis measured by in vivo incorporation of [3H] of tritiated water into fatty acids of liver and of perirenal and dorsal subcutaneous adipose tissues. In the adipose tissues, the specific activities of the three enzymes rather closely followed fluctuations in the rate of fatty acid synthesis. In the liver, ACX and especially ME activities were satisfactory indicators of de novo lipogenesis; G-6-PD activity did not depend on de novo lipogenesis.

Acetyl-CoA Carboxylase↗
PubMed1980

Disorganization of glycolytic and gluconeogenic pathways in skeletal muscle of aged persons studied by histometric and enzymatic methods.

Histometric data obtained by the point counting method, and the enzyme patterns of glycolysis, gluconeogenesis, fatty degradation and energy transfer have been determined in the same muscle specimens of m. vastus lateralis from 12 untrained patients between the ages of 4 and 78 years who suffered no disturbance of the neuromuscular system. Activities of 18 enzymes have been related to pure muscle weight corrected for fatty and connective tissue content, as well as to single fibre weight. A comparable muscle enzyme pattern was found in persons of around 20 years old and around 70 years old when expressed per gram of single fibre weight. However, in terms of grams of pure muscle weight, a significant activity decrease with age was obtained for 6-phosphofructokinase, triosephosphate dehydrogenase and phosphoenolpyruvate carboxykinase, whereas activity of hexose diphosphatase increased with age as also did 3-hydroxyacyl-CoA dehydrogenase activity. Five other cytoplasmic enzyme activities involved in glycolysis and energy transfer did not change significantly with age, nor did lysosomal acid phosphatase. The mitochondrial enzyme activities of gluconeogenesis (for example, pyruvate carboxylase, malic enzyme) were diminished to a lesser extent as also the auxiliary enzymes glutamic-oxaloacetic transminase and glutamic-pyruvic transaminase; glutamate dehydrogenase activity remained unchanged. The findings indicate a distinct disorganization of cytoplasmic glycolysis and gluconeogenesis pathways in presenile human skeletal muscle, confirming the histometric data already described. They cannot be explained by changes with age in numerical or areal ratio of type I and type II fibres.

Adolescent↗
PubMed2000

Hyperproliferative hepatocellular alterations after intraportal transplantation of thyroid follicles.

The thyroid hormone 3,5,3'-triiodo-L-thyronine (T3) is a strong direct hepatocyte mitogen in vivo. The effects of T3 resemble those of peroxisome proliferators, which are known to induce hepatocellular tumors in rats. With the aim of studying long-term local effects of thyroid hormones on liver parenchyma, small pieces of thyroid tissue were transplanted via the portal veins into the livers of thyroidectomized male Lewis rats. At 1 week, 3 weeks, 3 months, and 18 months after transplantation, the transplants were found to proliferate, to synthesize thyroglobulin, and to release thyroxine and T3. At 3 and 18 months after transplantation, the hepatocytes of the liver acini downstream of the transplanted follicles showed an increase in cytoplasmic basophilia, a loss of glycogen, an enlargement and hyperchromasia of their nuclei, and a strong increase in cell turnover compared with unaltered liver acini. The altered hepatocytes exhibited an increase in the activities of glucose-6-phosphate dehydrogenase, glucose-6-phosphatase, malic enzyme, mitochondrial glycerol-3-phosphate dehydrogenase, cytochrome-c-oxidase, and acid phosphatase; the activities of glycogen synthase and glycogen phosphorylase were strongly decreased. The hepatocytic alterations downstream of the transplanted follicles could be explained by effects of T3. On the other hand, they resembled alterations characteristic of amphophilic preneoplastic liver foci observed in different models of hepatocarcinogenesis.

Animals↗
PubMed1982

Intermediary carbohydrate metabolism in protoscoleces of Echinococcus granulosus (horse and sheep strains) and E. multilocularis.

With few exceptions, the specific activities of the glycolytic enzymes and the steady-state content of glycolytic and associated intermediates in protoscoleces of the horse (E.g.H) and sheep (E.g.S) strains of Echinococcus granulosus and the closely related E. multilocularis (E.m.) are very similar. Phosphorylase, hexokinase, phosphofructokinase and pyruvate kinase catalyse non-equilibrium reactions and the patterns of activity for pyruvate kinase, phosphoenolypyruvate carboxykinase and malic enzyme are similar in the three organisms. The levels of tricarboxylic acid cycle intermediates in E.g.H., E.g.S. and E.m. are of the same order as those reported in tissues with an active cycle. Each has a complete sequence of cycle enzymes but there are substantial differences between the three parasites with regard to the activity of individual enzymes. The activities of NAD and NADP-linked isocitrate dehydrogenases are significantly lower in E.g.H. than in E.g.S. and particularly in E.m. which suggests that the tricarboxylic acid cycle may play a more important role in carbohydrate metabolism and energy production in the latter parasites. Nevertheless, the three organisms utilize fermentative pathways for alternative energy production, fix carbon dioxide via phosphoenolpyruvate carboxykinase and have a partial reversed tricarboxylic acid cycle. It is speculated that in vivo more carbon will be channelled towards oxaloacetate than pyruvate at the phosphonenolpyruvate branch point. The steady state content of ATP and the ATP/AMP ratios are low in the three organisms, suggesting a low rate of ATP utilization in each.

Adenosine Triphosphate↗
PubMed1975

Regulation of oxaloacetate, aspartate, and malate formation in mesophyll protoplast extracts of three types of c(4) plants.

The use of mesophyll protoplast extracts from various C(4) species has provided an effective method for studying light-and substrate-dependent formation of oxaloacetate, malate, and asparate at rates equivalent to whole leaf C(4) photosynthesis. Conditions regulating the formation of the C(4) acids were studied with protoplast extracts from Digitaria sanguinalis, an NADP-malic enzyme C(4) species, Eleusineindica, an NAD-malic enzyme C(4) species, and Urochloa panicoides, a phosphoenolpyruvate (PEP) carboxykinase C(4) species. Light-dependent induction of CO(2) fixation by the mesophyll extracts of all three species was relatively low without addition of exogenous substrates. Pyruvate, alanine and alpha-ketoglutarate, or 3-phosphoglycerate induced high rates of CO(2) fixation in the mesophyll extracts with oxaloacetate, malate, and aspartate being the primary products. In all three species, it appears that pyruvate, alanine, or 3-phosphoglycerate may serve as effective precursors to the formation of PEP for carboxylation through PEP-carboxylase in C(4) mesophyll cells. Induction by pyruvate or alanine and alpha-ketoglutarate was light-dependent, whereas 3-phosphoglycerate-induced CO(2) fixation was not.Several differences between these species representing the three C(4) groups were observed. Substrate induction of CO(2) fixation in mesophyll protoplast extracts of D. sanguinalis gave malate as a major product; only by an apparent exchange reaction with cold aspartate did substantial label appear in aspartate (up to 53% of labeled products). In contrast, aspartate was a major product when alanine and alpha-ketoglutarate served as inducing substrates with E. indica (up to 57%) and U. panicoides (up to 86%). With induction by pyruvate or 3-phosphoglycerate, mesophyll preparations of U. panicoides and E. indica were less effective in forming malate (up to 31% of products) than D. sanguinalis (up to 87% of products). After 2 seconds of whole leaf (14)CO(2) fixation, malate was the major labeled product (57%) with D. sanguinalis, whereas with E. indica and U. panicoides aspartate was the predominant product (73% and 76%, respectively).With mesophyll protoplast extracts of D. sanguinalis, aspartate inhibited CO(2) fixation (about 50% at 0.6 mm), while malate was relatively uninhibitory at comparable concentrations. CO(2) fixation by mesophyll protoplast extracts of E. indica was inhibited by malate (about 50% at 0.6 mm), while aspartate was relatively uninhibitory. With mesophyll preparations of U. panicoides, malate or aspartate (2 mm) caused only slight inhibition of CO(2) fixation. The regulation of aspartate and malate synthesis in C(4) mesophyll cells is discussed relative to initial products of photosynthesis in C(4) species in vivo and species differences in the mechanisms of C(4) photosynthesis.

Journal Article↗
PubMed1985

Enzymes of glucose metabolism in Frankia sp.

Enzymes of glucose metabolism were assayed in crude cell extracts of Frankia strains HFPArI3 and HFPCcI2 as well as in isolated vesicle clusters from Alnus rubra root nodules. Activities of the Embden-Meyerhof-Parnas pathway enzymes glucokinase, phosphofructokinase, and pyruvate kinase were found in Frankia strain HFPArI3 and glucokinase and pyruvate kinase were found in Frankia strain HFPCcI2 and in the vesicle clusters. An NADP+-linked glucose 6-phosphate dehydrogenase and an NAD-linked 6-phosphogluconate dehydrogenase were found in all of the extracts, although the role of these enzymes is unclear. No NADP+-linked 6-phosphogluconate dehydrogenase was found. Both dehydrogenases were inhibited by adenosine 5-triphosphate, and the apparent Km's for glucose 6-phosphate and 6-phosphogluconate were 6.86 X 10(-4) and 7.0 X 10(-5) M, respectively. In addition to the enzymes mentioned above, an NADP+-linked malic enzyme was detected in the pure cultures but not in the vesicle clusters. In contrast, however, the vesicle clusters had activity of an NAD-linked malic enzyme. The possibility that this enzyme resulted from contamination from plant mitochondria trapped in the vesicle clusters could not be discounted. None of the extracts showed activities of the Entner-Doudoroff enzymes or the gluconate metabolism enzymes gluconate dehydrogenase or gluconokinase. Propionate- versus trehalose-grown cultures of strain HFPArI3 showed similar activities of most enzymes except malic enzyme, which was higher in the cultures grown on the organic acid. Nitrogen-fixing cultures of strain HFPArI3 showed higher specific activities of glucose 6-phosphate and 6-phosphogluconate dehydrogenases and phosphofructokinase than ammonia-grown cultures.

Actinomycetales↗
PubMed1997

Improved estimation of anaplerosis in heart using 13C NMR.

Anaplerotic enzymes, such as pyruvate carboxylase or malic enzyme, catalyze reactions that fill up the pools of the citric acid cycle (CAC), thereby increasing the total mass of CAC intermediates. Relative anaplerosis (y) denotes the ratio of anaplerotic flux to the flux catalyzed by citrate synthase. We examine conventional methods [C. R. Malloy, A. D. Sherry, and F. M. H. Jeffrey. J. Biol. Chem. 263:6964-6971, 1988; C. R. Malloy, A. D. Sherry, and F. M. H. Jeffrey. Am. J. Physiol. 259 (Heart Circ. Physiol. 28): H987-H995, 1990] of measurement of y using 13C-labeled precursors and analysis of [13C]glutamate labeling by nuclear magnetic resonance (NMR) spectroscopy. Through mathematical analysis and computer simulation, we show that isotopic enrichment of the pool of pyruvate that is substrate for anaplerosis will severely decrease the accuracy of estimates of y made with conventional methods no matter how small the mass of the pool of pyruvate. Suppose that the recycling parameter R denotes the fraction of molecules of pyruvate that contain carbons derived from intermediates of the CAC. Each means of estimation of relative anaplerosis in the peer-reviewed literature assumes that R = O, although this assumption has not been confirmed by experiment. We show that conventional formulas, using either fractional enrichments of carbons or isotopomer analysis, actually estimate at most y.(1 - R) instead of y during administration of [2-13C]acetate and unlabeled pyruvate. Using a new formula for estimation of y, we recalculate values of y from the literature and find them approximately 50% too low. We assume that all anaplerosis is via pyruvate and that the difference in isotopic enrichment between cytosolic and mitochondrial malate is negligible.

Animals↗
PubMed1976

[Enzyme activity of the bile and liver after disruption of its innervation and bile loss].

Continuous loss of bile in rats with a bile reservoir applied to the common bile duct caused an increase in specific activity of malic dehydrogenase, lactic dehydrogenase, glutamic dehydrogenase, glucose-6-phosphoric dehydrogenase, alkaline and acid phosphatase, urokinase and histidinase in the liver homogenates by the 7th day; the specific activity decreased by the 10th day. Disruption of innervation of the liver caused a sharp decrease of the ATP content and the abovementioned specifc activity in this organ. In continuous loss of bile there were revealed oscillations in the activity of the above-mentioned enzymes and sorbitol dehydrogenase in bile from the 1st to the 10th day of the experiment. Marked changes in the oscillations in the dysinnervated liver were in favour of the fact that those oscillations coursed under the control of the nervous system.

Adenosine Triphosphate↗