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1.
  • 1.1. Immature carp were subjected to 2-month fasting periods. Mobilization of reserves in liver and muscle, and the energy contribution of each reserve were studied. Changes in plasma glucose, amino acids, insulin and glucagon levels were determined throughout the experiment.
  • 2.2. No changes were observed in plasma glucose, insulin or glucagon at 19 days of fasting, but plasma amino acids increased. At 50 days of fasting, both plasma glucagon and amino acids increased, liver glycogen decreased and muscle proteolysis began.
  • 3.3. Between 50 and 67 days of fasting, plasma glucose and insulin decreased significantly, while glucagon and amino acids continued to increase. Strong muscular proteolysis was observed while liver glycogen stabilized.
  • 4.4. The contribution of each reserve in liver and muscle to energy production throughout fasting is considered.
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2.
  • 1.1. Changes in the glycogen content, condition, stomach content and acetic acid concentration of mussels Mytilus edulis and cockles Cerastoderma edule were followed during periods of up to 14 days of exposure (to air) at temperatures of 5 and 20°C.
  • 2.2. In animals with a high glycogen content the glycogen is not used during the first 3 to 7 days, at high and low temperature respectively.
  • 3.3. After this latent period the glycogen concentration often decreased, coinciding with a high mortality and an increase of the concentration of acetic acid.
  • 4.4. In cockles with a low glycogen content, and kept at a high temperature, glycogen can be used from the beginning of the stress period.
  • 5.5. Between species no clear differences were found.
  • 6.6. The stomach content decreased during exposure; however, the stomach content amounted to only 0.5 to 0.7% of the body weight, and is thought to be of minor importance as an energy source during the stress period.
  • 7.7. Especially at the higher temperatures glycogen finally is transformed into acetic acid.
  • 8.8. It is concluded that during exposure, the animals do not die because of a lack of energy reserves, but because of a high accumulation of acids.
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3.
  • 1.1. The major metabolic changes associated with repeated capture, aquarium transfer, anaesthesia and blood sampling were investigated in an Australian freshwater fish, the golden perch (Macquaria ambigua),
  • 2.2. A compounded stress response was seen after repetition of the procedure, in which the plasma glucose rose within 3 hr and amino acid concentrations rose and the serum free fatty acids concentration fell after 24 hr.
  • 3.3. Alanine was identified as an important circulating energy store in the stress response of golden perch.
  • 4.4. No change was noted in the serum protein, plasma lactate or β-hydroxybutyrate concentrations, indicating that tissue damage and hypoxia were absent, and that degradation of free fatty acids did not produce metabolites excess to the requirements of gluconeogenesis and the tricarboxylic acid cycle.
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4.
  • 1.1. The effects of a high-fat, high-energy diet and essential plus semi-essential amino acid gavage on pup rats have been studied (60–65 animals).
  • 2.2. The activities of alanine transaminase, adenylate deaminase, glutamine synthetase and serine dehydratase have been tested in liver and muscle.
  • 3.3. Plasma was used for the estimation of proteins, urea, amino acids, glucose, lactate, 3-hydroxy-butyrate and acetoacetate.
  • 4.4. Liver and muscle glutamine synthetase activities are increased by diet and gavage administered. Hepatic serine dehydratase is inhibited by a cafeteria diet but activated by amino acid gavage. Adenylate deaminase is inhibited by diet and gavage in the liver, but gavage does not affect this enzyme activity in muscle. Liver alanine transaminase is increased by the diet; in the muscle, cafeteria diet and amino acid gavage showed the highest values for this enzyme.
  • 5.5. In the plasma, the increase in lactate produced by the diet is inhibited by the amino acids provided. Cafeteria-fed pups showed lower urea levels and higher 3-hydroxybutyrate concentrations in the plasma.
  • 6.6. Intracellular glucose is diminished by cafeteria diet. In contrast, the blood cell amino acid concentration increases with diet and gavage supplied.
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5.
  • 1.1. Several pathways of carbohydrate metabolism were evaluated in three different tissues—liver, gonad and kidney—of a hatchery-reared population of rainbow trout (Oncorhynchus mykiss) which characterised two different stages of their gonadal maturation, i.e. previtellogenesis and established exogenous vitellogenesis.
  • 2.2. A fall in liver glycogen levels was observed during exogenous vitellogenesis. A decrease in activity of the enzymes involved in glycolysis and in the pentose phosphate shunt was also observed, suggesting that at the end of exogenous vitellogenesis the necessity of energy and reducing power has decreased compared to the situation at the onset of this period.
  • 3.3. The main changes observed in gonad during vitellogenesis were the decreased activity of glycolysis and the pentose phosphate shunt as well as increased glycogen levels. The stored glycogen should be used later in association with the embryo development.
  • 4.4. No major changes were observed in kidney metabolism throughout the vitellogenic process.
  • 5.5. Exogenous vitellogenesis in rainbow trout is mainly associated with increased glycogen levels in the gonad and decreased metabolic activity in the liver.
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6.
  • 1.1. A novel glycogen phosphorylase inhibitor was partially purified from crayfish hepatopancreas.
  • 2.2. The inhibitor was found only in two species of crayfish examined, and not in lobster, fresh and salt water clams, mussels or cockroaches.
  • 3.3. The inhibitor is a small protein (Mr = 23,000) which did not show proteolytic activity.
  • 4.4. Preliminary kinetic analysis of the inhibitory mechanism indicated that it bound to both glycogen and the glycogen phosphorylase protein.
  • 5.5. Inhibitor binding to glycogen resulted in a competitive inhibition pattern with respect to glycogen phosphorylase (inhibition constant of ca 10 μg/ml).
  • 6.6. The inhibitor also bound glycogen phosphorylase directly with a binding coefficient of 100 μg/ml resulting in a partially non-competitive inhibition pattern with respect to phosphate.
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7.
  • 1.1. This Mini Review deals with the metabolic consequences of administration of the hormone cortisol on proteins, carbohydrates and lipids in teleost fish.
  • 2.2. Many effects of administered cortisol on intermediary metabolism in fish have been reported: inhibition of protein synthesis and/or catabolism of tissue protein which result in higher availability of amino acids, induction of gluconeogenesis and of liver aminotransferases, hyperglycemia and glycogen deposition in the liver, induction of gluconeogenic enzymes, liberation of free fatty acids and deposition of liver lipids. All these effects are observed to a greater or less extent. However, the experimental data show that some effects are inconsistent.
  • 3.3. Some explanations for the inconsistencies are given.
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8.
  • 1.1. The actions of piroxicam, a nonsteroidal and noncarboxylic anti-inflammatory drug, on the metabolism of the isolated perfused rat liver were investigated. The main purpose was to verify if piroxicam is also active on glycogenolysis and energy metabolism, as demonstrated for several carboxylic nonsteroidal anti-inflammatories.
  • 2.2. Piroxicam increased oxygen consumption in livers from both fed and fasted rats.
  • 3.3. Piroxicam increased glucose release and glycolysis from endogenous glycogen (glycogenolysis).
  • 4.4. Gluconeogenesis from lactate plus pyruvate was inhibited.
  • 5.5. The action of piroxicam on oxygen consumption was blocked by antimycin A, but not by atractyloside.
  • 6.6. The action of piroxicam in the perfused rat liver metabolism seems to be a consequence of its action on mitochondria.
  • 7.7. It can be concluded that inhibition of energy metabolism and stimulation of glycogenolysis are not specific properties of carboxylic nonsteroidal anti-inflammatory drugs.
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9.
  • 1.1. NADH-dependent isocitrate dehydrogenase has been purified 110-fold from the crude extract of the flight muscle mitochondria of Aldrichina grahami.
  • 2.2. The purification procedure involved Triton X-100 treatment of isolated mitochondria, column chromatography on DEAE-cellulose, Affi-gel blue, and P-cellulose.
  • 3.3. The purified enzyme was homogeneous by criteria of the polyacrylamide gel electrophoresis.
  • 4.4. The enzyme of the blowfly contains more acidic amino acids and less hydrophobic amino acids than that of pig heart.
  • 5.5. The molecular weight was determined to be 330,000 daltons. The subunit construction differs from ghat of mammalian isocitrate dehydrogenase.
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10.
  • 1.1. In lobster hepatopancreas, extracellular protreases cause the inactivation of glycogen phosphorylase.
  • 2.2. The proteolysis of glycogen phosphorylase purified from rabbit muscle by these proteases has been shown by SDS-polyacrylamide gel electrophoresis.
  • 3.3. A cell isolation technique has allowed us to remove proteases of extracellular digestion and to measure glycogen phosphorylase activity in lobster hepatopancreas.
  • 4.4. The glycogen phosphorylase activity seems to be mainly associated with R cells while it could not be detected in B cells.
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11.
  • 1.1. Glycine, proline, and taurine are the quantitatively most important amino acid osmolytes in Penaeus aztecus postlarvae.
  • 2.2. Taurine dominates the amino acid pool in low salinity, while proline dominates the amino acid pool at higher salinities.
  • 3.3. Although not major contributors to the pool, glutamate and alanine are constitutively synthesized from [14C]glucose and [14C]glutamate under constant salinity and under hyperosmotic stress treatments.
  • 4.4. Proline synthesis from [14C]-precursors is apparent under constant high (but not low) salinity and is significantly induced by hyperosmotic stress.
  • 5.5. No appreciable glycine synthesis was observed from [14C]glucose or [14C]glutamate under any experimental conditions.
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12.
  • 1.1. Intestines of fresh and dehydrated-starved L. terrestris were compared to tissue and anterior-posterior distribution of glutamate dehydrogenase (GDH) and other mitochondrial or cytosol dehydrogenases.
  • 2.2. For any dehydrogenase, including GDH, practically all the activity was in the gut epithelium. This distribution of GDH supports Tillinghast (1967, 1968) as to the excretory route for ammonia.
  • 3.3. While the distributions of the marker dehydrogenases were reasonably uniform along the intestine, the GDH activity was predominantly (80–90% of the total activity) in the last third of the mid-intestine, indicating a true physiological differentiation of the midgut tube. The GDH activity of the typhlosole was about two times the activity in the peripheral epithelium. The GDH distribution was independent of the physiological state of the worm.
  • 4.4. From the distribution of GDH it follows that the mid-intestine, immediately before the hindgut, is the main region both for amino acid uptake and catabolism. As regards amino acids, it typifies the primitive digestive tube by having both the absorptive and the liver functions.
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13.
  • 1.1. Eel were exposed to a sublethal concentration of lindane (0.335 ppm) for 6, 12, 24, 48, 72 and 96 hr.
  • 2.2. Concentrations of glycogen, glucose, lactate, pyruvate and lipids were determined in gill tissue after lindane exposure.
  • 3.3. Gill glycogen descreased and glucose levels increased at 6 hr of treatment, lactate and pyruvate concentration increased between 6 and 48 hr. Total lipid values decreased between 6 and 24 hr; thereafter, the levels increased up to 72 hr of exposure.
  • 4.4. Clear changes were found in all parameters tested in gill tissues. The observed effects of lindane on metabolism in fish are discussed in relation to acute stress syndrome.
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14.
  • 1.1. A glycogen/protein complex which contains the major portion of glycogen synthase activity in Ascaris suum muscle has been purified.
  • 2.2. The complex contains two proteins which can be dissociated from a glycoprotein component.
  • 3.3. The glycoprotein contains glycogen-like domains and is resistant to trypsin digestion.
  • 4.4. The glycogen synthase activity in the purified complex catalyzes glycogen synthesis in the absence of exogenous glycogen, but demonstrates an absolute glucose 6-phosphate requirement for activity.
  • 5.5. The data support the hypothesis that this isozyme of glycogen synthase is significantly different from the cyclic AMP-regulated enzyme.
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15.
  • 1.1. The glycogen content of the mantle tissue reached a maximum in the summer (May–July) with levels of 41.0–53.5% of the dry tissue weight.
  • 2.2. Seasonal changes in glycogen synthetase activity showed that the I-activity (independent of G6P) increased up to 10-fold in June as compared with December. The measured I-activity of glycogen synthetase was sufficient to account for the accumulation of mantle glycogen in the summer.
  • 3.3. The I-activity of glycogen synthetase declined rapidly in July of each year. A possible role for the inhibition of glycogen synthetase by high levels of tissue glycogen is suggested.
  • 4.4. The I-activity in the mantle tissue of mussels on the shore was higher than that for animals starved in the laboratory for 2–3 days. The differences were minimal in early May but increased markedly in late May–July. Starved mussels returned to the shore showed an increase in I-activity of glycogen synthetase.
  • 5.5. Injection of 30 μmol glucose into the adductor muscle increased the concentration of glucose in the mantle fluid to 2.0–2.5 mM. A similar injection of 60 μ mol glucose resulted in a time-dependent increase in the I-activity of glycogen synthetase.
  • 6.6. Injection of mussels with mammalian insulin or anti-insulin serum had no effect on the activity of glycogen synthetase. Our results are at variance with those of other workers who have used the mammalian hormone in molluscan studies (see Discussion).
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16.
  • 1.1. 13C-NMR spectra of formic acid solutions of chitin proteoglycans from cephalopod pen, lamellibranch siphon sheath and crab cuticle have been determined.
  • 2.2. Carbohydrate and amino acid components provide well-defined resonances, completely assignable in the case of hexosamine and partially so for protein amino acids.
  • 3.3. The individually unique spectra contain information of compositional and chain environment nature.
  • 4.4. Spectral data for each protein amino acid, as a formic acid solution, is presented and compared with values for chemical shifts of amino acids and peptides in water.
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17.
  • 1.1. The photoregulation shown by glyceraldehyde 3-phosphate dehydrogenase and glucose 6-phosphate dehydrogenase appears to be independent of the mad gene product(s) and also independent of carotene biosynthesis regulation.
  • 2.2. The photoregulation of malate dehydrogenase appeared to be dependent on the mutation of the mad and car S genes.
  • 3.3. Pyruvate kinase and lactate dehydrogenase may be classified as light-independent.
  • 4.4. The action of ATP and fructose 1,6-bisphosphate on the enzymes studied was generally independent of light/dark grown conditions.
  • 5.5. However, the effect of fructose 1,6-bisphosphate on Phycomyces pyruvate kinase appears to be light-dependent.
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18.
  • 1.1. Activities of the three ammonia-forming enzymes, glutamate dehydrogenase, AMP deaminase and serine dehydrase (SerDH), were measured in tissues of gill, digestive diverticula, mantle and foot muscle of the brackish-water bivalve Corbicula japonica.
  • 2.2. High levels of SerDH activity were detected in gill and digestive diverticula, while the activity levels of the other two enzymes were low.
  • 3.3. The result suggests the significance of SerDH in amino acid degradation of this species.
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19.
  • 1.1. The d-lactate dehydrogenase from Leuconostoc lactis has been purified in high yield.
  • 2.2.The enzyme is a dimer of subunits of Mr = 39,000 and each subunit contains a single thiol group. The N-terminal residue is methionine.
  • 3.3. The amino acid composition has been determined and is typical of that of a soluble globular protein.
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20.
  • 1.1. Four ostrich pancreatic α-amylase isoenzymes were isolated by isoelectric focusing, following affinity chromatography on cyclohepta-amylose-Sepharose 4B.
  • 2.2. Amino acid compositions of the four isoenzymes are very similar with only one charged amino acid (Arg) being significantly different.
  • 3.3. The molecular weights, as determined by SDS-PAGE and amino acid composition, are nearly identical (52–53 kDa) for all four isoenzymes.
  • 4.4. The four α-amylase isoenzymes appear to be kinetically distinct enzymes with a requirement for calcium.
  • 5.5. Ostrich α-amylase isoenzymes appear to be non-glycosylated and contain one free thiol group.
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