Atrial natriuretic peptides in the heart and hemolymph of the oyster,Crassostrea virginica: A comparison with vertebrates

• 1.1. The content of atrial natriuretic peptides (ANPs) in the auricles of oysters, Crassostrea virginica, was significantly (P < 0.01) greater than in their ventricles.
• 2.2. High-performance gel permeation chromatography (HP-GPC) followed by ANF radioimmunoassay revealed two peaks in both oyster and vertebrate (rat) hearts—a major peak where the 12.6–14 kDa ANF prohormone elutes and a smaller peak where the pure human form of ANF elutes.
• 3.3. HP-GPC evaluation followed by proANF 31–67 radioimmunoassay revealed only an ANF-like prohormone while HP-GPC followed by proANF 1–30 radioimmunoassay revealed the ANF prohormone and a proANF 1–30-like peptide in oyster and rat hearts.
• 4.4. ANPs concentrations in hemolymph were 940 ± 129, 225 ± 25, and 100 ± 10 pg/ml by the proANF 1–30, proANF 31–67, and ANF radioimmunoassays, respectively.
• 5.5. Atrial natriuretic-like peptides are present in the oyster heart in molecular species similar to vertebrate species and these peptides are also present in hemolymph.

     

The calcium uptake by larvae of the oyster,Crassostrea virginica,and the clam,Mulinia lateralis

• 1.1. The uptake of calcium by larvae of the oyster (Crassostrea virginica) and the clam (Mulinia lateralis) was measured using the ⁴⁵Ca isotope tracer method.
• 2.2. An equation was established for the calculation of true calcium uptake and the rates expressed as ng Ca/larva/hr were 0.39 and 0.34 ± 0.16 (n = 4) for 3- and 11-day-old oyster larvae, and 0.03 and 0.15 for 7- and 9-day-old clam larvae, respectively.
• 3.3. This system is sensitive, rapid, simple and potentially useful for the measurements of calcium metabolism, shell formation, aquaculture and toxicity.

     

A comparison of aspartate transcarbamylase activity in juvenile pacific oysters (Crassostrea gigas) when fed various diets

• 1.1. The optimum pH for measurement of aspartate transcarbamylase activity in oyster tissue was determined to be 9.35 while the optimum temperature was 39.5°C.
• 2.2. Aspartate transcarbamylase activity varied significantly over short periods of time (hr) possibly due to fluctuations in the amount of food digested.
• 3.3. The composition of the oyster's diet also affected the levels of aspartate transcarbamylase activity in oyster tissues.
• 4.4. Those oysters fed an egg yolk-starch diet contained significantly lower aspartate transcarbamylase activity than oysters fed an egg yolk-starch-salmon oil diet or a casein-starch-salmon oil diet.
• 5.5. The aspartate transcarbamylase activities in oysters fed Phacedactylum tricornutum or a starch diet were not significantly different from the activities in oysters fed the egg yolk-starch diet.

     

Reabsorption and accumulation of α-amino-iso-butyric acid in the nephridia of Sabella pavonina Sa vigny (Annelida polychaeta)

• 1.l. High amino acid concentrations were found in the anterior coelomic fluid of a Polychaeta (Sabella pavonina Savigny).
• 2.2. The concentrations being much higher in the fluid which penetrates the nephrostomia into the nephridia lumen than in the final urine indicates that the nephridia reabsorbs large amounts of amino acids.
• 3.3. Nephridial perfusion experiments showed that an amino acid analogue (α-amino-iso-butyric acid, AIB) is transported by the nephidia.
• 4.4. The transport took place across the nephridial wall owing to the presence of a carrier-mediated transport system and a diffusion system.
• 5.5. For the carrier-mediated transport, the V_max was 0.234 ± 0.025 nmol·min⁻ and the K_m 3.715 ± 0.315mmol·l⁻.
• 6.6. AIB accumulated in the nephridial cells up to a maximum rate of 01.17 nmol·min⁻.
• 7.7. Intracellular accumulation stopped increasing when the V_max for reabsorption was reached.
• 8.8. These results indicate that the carrier-mediated transport of AIB is located at the apical membrane of the nephridial cell, and that AIB transport by simple diffusion takes place through the paracellular pathway.

     

Effect of starvation and experimental feeding on the proximate composition and caloric content of an antarctic teleost,Notothenia coriiceps neglecta

• 1.1. Starving Notothenia coriiceps nn/lecta at 1°C for 20 days resulted in a loss of 4.22 gcal/kcal per day.
• 2.2. During starvation energy was obtained from lipid and carbohydrate stores of the liver and red muscle.
• 3.3. Feeding N. coriiceps neglecta low lipid, high protein shrimp meat at 18.9 gcal/kcal per day at 1°C for 20 days resulted in a gain of 8.5 gcal/kcal per day.
• 4.4. The level of carbohydrate in the liver and red muscle increased five times.
• 5.5. Gross growth efficiency (K₁) equalled 0.52.
• 6.6. Net growth efficiency (K₂) equalled 0.67.

     

Thermostability and activation by divalent cations of the membrane-bound inorganic pyrophosphatase of Rhodospirillum rubrum

• 1.1. The activation energy of the membrane bound H⁺-pyrophosphatase is 44.9 k J·mol⁻¹, for the detergent solubilized enzyme is 55.9 kJ·mol⁻¹.
• 2.2. The Arrhenius plots obtained for pyrophosphatases of Rhodospirillum rubrum show no breaks.
• 3.3. At 70°C, the membrane-bound pyrophosphatase is more stable in the presence of either Mg²⁺ or Zn²⁺ than in their absence.
• 4.4. At 65°C, an activator effect of Mg²⁺ or Zn²⁺ was observed. Nevertheless, at 70°C no activation was obtained.
• 5.5. The activator effects of Mg²⁺ or Zn²⁺ were depended of their concentration.

     

Seasonal changes of lipids and fatty acids in oyster tissues (Crassostrea virginica) and estuarine particulate matter

• 1.1. Lipid concentration in adductor muscle ranged from 2–68, in visceral mass from 5–28, in mantle and gill from 5–20 and in heart from 27.8–79 mg/g wet tissue. Particulate matter lipids varied from 1.0–2.6 mg/1 of estuarine water.
• 2.2. Neutral and polar lipids ranged from 25–38% of the total lipids in the oyster tissue and from 62–75% of the estuarine particulate organic matter.
• 3.3. Seasonal maxima of lipid concentrations varied among oyster tissues. Peak particulate lipids occurred in November.
• 4.4. It is proposed that seasonal variation in oyster lipids was more related to reproductive cycles than to food lipid supply.

     

The peculiarities of nitrogen excretion in sturgeons (Acipenser ruthenus) (Pisces,Acipenseridae)—I. the influence of ration size

• 1.1. The nonfaecal nitrogenous excretion rate in starved sterlet fingerlings and fingerlings fed on different rations was investigated. The weight of the fish and temperature of the water was 43 g and 17.5°C, respectively.
• 2.2. In the nonfaecal excrements of starved sterlets the ammonia: urea ratio was substantially lower than in teleosts. This ratio was found to be 1.4:1.
• 3.3. In fed sterlets the urea excretion rate was higher than in starved ones but independent of ration size.
• 4.4. During the day the urea excretion rate in sterlets was constant.
• 5.5. The ammonia excretion rate accelerated 2 hr after feeding and reached its peak duration 6–11 hr after depending on the ration size.
• 6.6. Total ammonia output in the sterlet increased following the increase of ration size up to 8.4% of body wt. Further increases in ration size did not cause the corresponding elevation of ammonia excretion rate.

     

Biochemical studies in a eunicid (polychaete) of the littoral of São Paulo,Brazil

• 1.1. The sodium, potassium, chloride, calcium, magnesium, phosphorus, sulphur, copper, iron, total carbon dioxide, uric acid, creatinine, urea, glucose, erythrocruoin, nitrogen, total iodine, protein-bound iodine, total lipids, triglycerides, alkaline phosphatase activity, acid phosphatase activity and copper oxidase activity contents of the blood of the giant Polychaete, Eunice sp., were determined.
• 2.2. The osmolarity of the blood was 997 mOsm/1 and the pH was 6·49, a very low value. The bicarbonate concentration estimated by the Henderson-Hasselbach equation was 4·70 mM/1.
• 3.3. The values of the sea water, sediments, water contained in the tube, tube, cuticle, muscle and faeces are also given.
• 4.4. The chemical composition of the mucus was determined.

     

Changes in molecular species compositions of glycerophospholipids in Japanese oyster Crassostrea gigas (Thunberg) during frozen storage

• 1.1. Changes in molecular species composition of phosphatidylethanolamine and phosphatidylcholine in Japanese oyster were studied during storage at −20°C.
• 2.2. In alkenylacyl- and alkylacyl-glycerylphosphorylethanolamine (GPE) and -glycerylphosphorylcholine (GPC), the molecular species having combinations of relatively shorter alkenyl and alkyl chains on sn-1 positions and 20:5n-3 on sn-2 positions, were lost rapidly in comparison with those of the corresponding longer alkenyl and alkyl chains and 22:6n-3.
• 3.3. In the case of diacyl-GPE, more molecular species having combinations of chains with longer total carbons (TC) and more double bonds (DB) were lost, than those having chains with shorter TC and fewer DB. Changes in the molecular species of the diacyl-GPC were opposite to those of the diacyl-GPE.
• 4.4. The results obtained suggest that oxidations and/or enzymatic hydrolyses selectivey occurred on the molecular species of glycerophospholipids during frozen storage.

     

Oxygen consumption and torpor in the fat-tailed dwarf lemur (Cheirogaleus medius): Rethinking prosimian metabolism

• 1.1. Oxygen consumption was measured in a lemuriform prosimian, Cheirogaleus medius. throughout a 24-hr cycle. The standard metabolic rate was determined to be 0.95 ml O₂ (g · hr)⁻¹ agreeing well with the value predicted by allometric equations, 0.91 ml O₂ (g · hr)⁻¹.
• 2.2. As a group, prosimians are argued to have metabolic levels in agreement with eutherian norms, rather than hypometabolic levels as previously supposed.
• 3.3. Day length is shown to be an important behavioral cue for this species. Its complex yearly and daily torpor cycles are linked to this stimulus.

     

Isolation and characterization of glutamine synthetase from the diazotroph Azospirillum brasilense

• 1.1. Glutamine synthetase was purified from the diazotroph Azospirillum brasilense.
• 2.2. The holoenzyme with a M_r of 630,000 is composed of 12 subunits of M_r 52,000.
• 3.3. A modified subunit of M_r 53,000 was also found by electrophoresis under denaturing conditions.
• 4.4. It is shown that the M_r 53,000 species is the adenylylated subunit.
• 5.5. The apparent K_m values for glutamate, ATP and ammonia were 2.5 ± 0.3 mM, 200 ± 20 μM and42 ± 2 μM, respectively.
• 6.6. Levels of glutamine synthetase activity in A. brasilense cells varied by a factor of 8 depending on the nitrogen source and its concentration in the growth medium.

     

Purification and properties of an ld-dipeptidase FROM Bacillus sphaericus

• 1.1. An ld-dipeptidase (EC 3.4.13.-) that hydrolyzes the unrelated dipeptides l-Ala-d-Glu (sp. act. 0.85 μmol·min⁻¹·mg⁻¹) and l-Lys-d-Ala (sp. act. 11 μmol · min⁻¹·mg⁻¹) has been purified 250-fold from the sporulation medium of Bacillus sphaericus with a 4% recovery of lytic activity.
• 2.2. Throughout the purification steps, followed with both substrates, the enzyme peaks of activities were congruent and the ratios of activities were constant. Both activities were activated 50-fold by cobalt. Polyacrylamide gel electrophoresis of the final preparation showed the two enzyme activities to be coincident. The data are consistent with those activities being due to a single enzyme.
• 3.3. Sodium dodecylsulfate polyacrylamide gel electrophoresis of the purified enzyme showed a single protein band (M_r 38,000).
• 4.4. This dipeptidase hydrolyzes some other ld-dipeptides with a free amino and carboxyl group. Although dipeptides having a di-amino acid as the amino terminus are the best of the substrates tested, the hydrolysis occurs also when neutral amino acids are N-terminal. The activity is higher with neutral C-terminal residues such as Gly or d-Ala than with a di-acid residue such as d-Glu.
• 5.5. This enzyme may have a function in peptidoglycan metabolism.

     

Increased muscle glucose uptake in response to chronic glyburide treatment is not related to changes in glucose transporter (GLUT4) protein

• 1.1. The mechanism of action of glyburide (a sulfonylurea) on muscle has been investigated by measuring glucose uptake and glucose transporter (GLUT4) protein levels after chronic glyburide treatment.
• 2.2. A dietary induced insulin resistant rat model (4 wk of high-fat, high-sucrose feeding) was given glyburide (2mg/kg/day) for 10 days and glucose uptake was measured in a perfused hindquarter preparation.
• 3.3. Protein levels of the GLUT4 glucose transporter were determined by Western analysis.
• 4.4. After 7 days of treatment, rats fed glyburide had lower blood glucose concentrations 2 hr (72 ± 5 vs 103 ± 12 mg/dl) and 24 hr (97 ± 7 vs 123 ± 7 mg/dl) after glyburide administration with no difference in serum insulin levels compared to vehicle treated animals.
• 5.5. Glucose uptake was approx doubled in basal state (0 insulin) in response to glyburide (2.8 + 0.4 vs 1.7 ± 0.2μ mol/g per hr).
• 6.6. Maximal insulin (100 nM) stimulated glucose uptake tended to be higher in the glyburide treated group, but did not reach statistical significance (8.0 ± 0.7 vs 7.0 ± 0.6 μmol/g per hr).
• 7.7. Western analysis revealed no significant effect of glyburide on the GLUT4 protein level in skeletal muscle.
• 8.8. These results suggest that glyburide alters glucose uptake through some mechanism other than alterations in the level of the GLUT4 glucose transporter protein.

     

Properties of sweat,burro (Equus asinus) and man

• 1.1. Sweat of two burros (Equus asinus) was collected after two desert walks, one at 38°C, one at 41°C.
• 2.2. Sweat from one burro was about twice as concentrated as from the other. In that respect and in respect to concentrations of chloride, sodium and potassium their sweat was like that of man.
• 3.3. Low concentrations of bicarbonate were present in burros' sweat contrasted with little if any in man's.
• 4.4. Urea nitrogen plus ammonia nitrogen were found in higher concentrations in burros' sweat than in man's sweat.

     

Chemical structures of mono-, di-, tri- and tetraglycosyl glycerides in rice bran

• 1.1. Monoglycosyl monoglyceride, mono-, di-, tri- and tetraglycosyl diglycerides were isolated from rice bran and characterized for their chemical structures.
• 2.2. Monoglycosyl monoglycerides were characterized as Gal(β1' → 3)-1- or 2-monoacyl-sn-glycerol and Glc(β1' → 3)-1- or 2-monoacyl-sn-glycerol.
• 3.3. The structures ofmonoglycosyl diglyceride were Gal(β1' → 3)-1,2-diacyl-sn-glycerol and Glc(β1' → 3)-1,2-diacyl-sn-glycerol. Epimeric separation of the galactosyl and glucosyl glycerides was for the first time achieved by thin-layer chromatography.
• 4.4. The main diglycosyl diglyceride was shown to be Gal(α1' → 6')-Gal(β1' → 3)-1,2-diacyl-sn-glycerol.
• 5.5. The major structure of triglycosyl diglyceride was characterized as Gal(α1″' → 6″)-Gal(α1″ → 6')-Gal(β1' → 3)-1,2-diacyl-sn-glycerol.
• 6.6. The representative structure of tetraglycosyl diglyceride was for the first time established as Gal(α1″ → 6″')-Gal(α1″' α 6″)-Gal(α1″ → 6')-Gal(βl' → 3)-1, 2-diacyl-sn-glycerol.

     

An alkaline phosphatase from Thermus sp strain Rt41A

• 1.1. A thermostable orthophosphoric monoester phosphohydrolase (EC 3.1.3.1) from Thermus sp strain Rt41A has been purified 400-fold to give a specific activity of 25 U/mg at 60°C in IM diethanolamine (pH 11.1).
• 2.2. The enzyme has a M_r of 160,000 and is trimeric.
• 3.3. The half-life of the enzyme is 5 min at 85°C.
• 4.4. The enzyme has a wide specificity for a number of phosphate monoesters.
• 5.5. The H_m of the enzyme is pH dependent, so the pH optimum of the enzyme is affected by the substrate concentration.
• 6.6. The enzyme is inhibited 50% by 20 mM Ca²⁺ or Mg²⁺.
• 7.7. The K_i for phosphate, EDTA-di sodium salt and arsenate (in 1 M diethanolamine, pH 11.1) is approx 1.2, 1.6 and 4mM respectively.
• 8.8. Urea (200 mM) is not inhibitory.

     

Influence of temperature,rate of feeding and body weight on nitrogen metabolism of bream,Abramis brama L

• 1.1. Measurements of the rate of nitrogen consumption, total nitrogen and ammonia excretion and nitrogen absorption of bream, Abramis brama L. (body weight range 0.4–519 g wet wt) were made at 10, 15 and 20 C.
• 2.2. Fish were fed once daily on live zooplankton collected in Lake Balaton and cultured Tubifex sp. at 5–15% of their body weight.
• 3.3. Fish size and temperature had a combined effect on the rate of total nitrogen excretion. Total nitrogen excretion did not increase proportionally with an increase in consumption.
• 4.4. On average, 52–80% of the nitrogen consumed with food was excreted by bream.
• 5.5. The greatest part of total nitrogen excretion was ammonia and its proportion in the total ranged between 53 and 75%.
• 6.6. Temperature did not have any significant effect on the proportion of excreted ammonia and the rate of excreted total nitrogen was the only factor determining its proportion in the total.
• 7.7. The rate of nitrogen absorption of bream was surprisingly very high.

     

Lipoxygenase of the thermophilic bacteria thermoactinomyces vulgaris—properties and study on the active site

• 1.1. A lipoxygenase activity was purified from Thermoactinomyces vulgaris and some of its properties were characterized.
• 2.2. The enzyme showed a temperature activity range of 40–55°C with still significant activity over 60°C.
• 3.3. The pH of activity on linoleic acid had a broad range with an optimum at pH 6.0 and a weaker one at pH 11.0.
• 4.4. On arachidonic acid the pattern was narrow bell-shaped with an optimum at pH 6.5.
• 5.5. The purified lipoxygenase from Th. vulgaris showed an apparent K_m of 1 mM and V_max of 0.84 μmol diene/min/mg protein.
• 6.6. It was inhibited by the oxidation products, 9-HPOD and 13-HPOD.
• 7.7. A 160,000 Da molecular weight of the enzyme was determined by molecular filtration. Methionine, tyrosine, tryptophan and cysteine are apparently involved in its activity.

     

Lysosomal acid deoxyribonuclease from vervet monkey livers—II: Enzymic properties

• 1.1. Primate liver lysosomal acid DNase is an endonucleolytic enzyme.
• 2.2. The enzyme has both 3'- and 5'-nucleotidohydrolase activities.
• 3.3. The oligonucleotides produced by DNase are polymers mainly about 30 mononucleotides long.
• 4.4. The Arrhenius plot shows a discontinuity with a transition temperature at 47°C, with an activation energy of 107 kJ/mol below and 67 kJ/mol above this temperature.
• 5.5. The activation enthalpy is 104kJ/mol and the entropy −0.498 kJ/mol/K.
• 6.6. The enzyme is subject to substrate inhibition and the K_m value is 159 × 10⁻³mM DNA-P.