Copper, nickel, and thallium uptake by the lichen Cladina rangiferina

1981 ◽  
Vol 59 (1) ◽  
pp. 91-100 ◽  
Author(s):  
M. A. S. Burton ◽  
P. LeSueur ◽  
K. J. Puckett
Keyword(s):  
Metal Uptake ◽  
Deionized Water ◽  
Metabolic Inhibitors ◽  
Temperature Dependent ◽  
Low Concentrations ◽  
Nickel Uptake ◽  
High Concentrations ◽  
Uptake Studies ◽  
Cladina Rangiferina ◽  
Very High

Metal uptake studies with Cladina rangiferina showed that the affinity for nickel was much lower than for copper or thallium. Nickel uptake was not decreased by the absence of light or oxygen or by pretreatment with metabolic inhibitors. Nickel uptake was not temperature dependent but was very dependent upon pH.Cation-exchange studies demonstrated that there was a stoichiometric exchange of Ni2+ for Sr2+, and Cu2+ for Sr2+. The exchange of Tl+ for Sr2+ was not stoichiometric, excess Tl+ was accumulated in relation to the Sr2+ released. The ratio of Sr2+:Tl+ exchange increased with increasing Tl+ availability from 1:9 (12.5 μmol Tl+ available/g of lichen) to 1:2 (500 μmol Tl+ available). Acid-treated lichen gave the expected exchange ratio of 1:2. Washing of the thalli with deionized water resulted in the continued loss of Tl+ from acid-treated and live C. rangiferina. Copper and nickel were not released in this manner.Increasing concentrations of copper and thallium produced a corresponding loss of potassium from the thallus. The potassium loss was initiated at low concentrations of copper and thallium whereas very high concentrations of manganese and nickel were required to bring about the same response.

scholarly journals Detection of endotoxins with the Limulus test in burned and unburned mice infected with different species of gramnegative bacteria

1975 ◽  
Vol 75 (1) ◽  
pp. 99-112 ◽  
Author(s):  
R. J. Jones ◽  
E. A. Roe ◽  
R. E. Dyster
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Low Concentrations ◽  
High Concentrations ◽  
Very High ◽  
Limulus Test

SUMMARYThe Limulus test detected endotoxins in the plasma of burned and unburned mice infected with different species of gram-negative bacteria. Individual strains of different species of gram-negative bacteria produced different amounts of endotoxin in the plasma of infected mice. Plasma from mice given lethal infections showed very high concentrations of endotoxin. Low concentrations of endotoxin in the plasma were tolerated by mice but high concentrations were invariably fatal. A polyvalent pseudomonas vaccine reduced endotoxin in the plasma of mice given lethal infections of Pseudomonas aeruginosa.

scholarly journals Temperature and the regulation of enzyme activity in poikilotherms. Properties of rainbow-trout fructose diphosphatase

1969 ◽  
Vol 111 (3) ◽  
pp. 287-295 ◽  
Author(s):  
H. W. Behrisch ◽  
P. W. Hochachka
Keyword(s):  
Enzyme Activity ◽  
Rainbow Trout ◽  
Temperature Adaptation ◽  
Temperature Dependent ◽  
Ph Optimum ◽  
Physiological Temperature ◽  
Low Concentrations ◽  
High Concentrations ◽  
Regulation Of Enzyme Activity ◽  
Hill Plots

1. The properties of fructose diphosphatase from the liver of rainbow trout (Salmo gairdnerii) were examined over the physiological temperature range of the organism. 2. Saturation curves for substrate (fructose 1,6-diphosphate) and a cofactor (Mg2+) are sigmoidal, and Hill plots of the results suggest a minimum of two interacting fructose 1,6-diphosphate sites and two interacting Mg2+ sites per molecule of enzyme. 3. Mn2+-saturation curves are hyperbolic, and the Ka for Mn2+, which inhibits the enzyme at high concentrations, is 50–100-fold lower than the Ka for Mg2+. 4. Fructose diphosphatase is inhibited by low concentrations of AMP; this inhibition appears to be decreased and reversed by increasing the concentrations of Mg2+ and Mn2+. Higher concentrations of AMP are required to inhibit the trout fructose diphosphatase in the presence of Mn2+. 5. The affinities of fructose diphosphatase for fructose diphosphate and Mn2+ appear to be temperature-independent, whereas the affinities for Mg2+ and AMP are highly temperature-dependent. 6. The pH optimum of the enzyme depends on the concentrations of Mg2+ and Mn2+. In addition, pH determines the Ka for Mg2+; at high pH, Ka for Mg2+ is lowered. 7. The enzyme is inhibited by Ca2+ and Zn2+, and the inhibition is competitive with respect to both cations. 8. The possible roles of these ions and AMP in the modulation of fructose diphosphatase and gluconeogenic activity are discussed in relation to temperature adaptation.

scholarly journals Etude, dans le raisin, de l'activité β-glucosidase

OENO One ◽  
1988 ◽  
Vol 22 (2) ◽  
pp. 125
Author(s):  
C. Biron ◽  
Robert Cordonnier ◽  
Ollivier Glory ◽  
Ziya Günata ◽  
Jean-Claude Sapis
Keyword(s):  
Plant Material ◽  
Grape Berry ◽  
Cabernet Sauvignon ◽  
Mature Fruit ◽  
Glucosidase Activity ◽  
Low Concentrations ◽  
High Concentrations ◽  
Grape Leaf ◽  
Method Of Extraction ◽  
Very High

<p style="text-align: justify;">Dans ce travail, on étudie l'activité β-glucosidase du raisin. Une méthode d'extraction de l'enzyme à partir du matériel végétal a été mise au point et optimisée. L'activité enzymatique est mesurée spectrophotométriquement avec le paranitrophénylglucopyranoside comme substrat. Dans la baie de raisin, la β-glucosidase est concentrée dans les parties solides, pellicule et pulpe. Dans le jus, elle est en faible quantité. Dans la feuille de vigne, l'activité est élevée dans le limbe, faible dans le pétiole. Au cours de la maturation du raisin l'activité β-glucosidase augmente jusqu'à la maturité. Au-delà, jusqu'au stade de surmaturation, elle reste constante. Dans les raisins mars, la β-glucosidase est présente dans toutes les variétés étudiées, aussi bien dans les variétés aromatiques (Muscat d'Alexandrie, Muscat de Frontignan, Muscat de Hambourg) que dans celles non aromatiques (Carignan, Grenache, Cinsaut, Baroque, Cabernet-Sauvignon, Syrah, Merlot). Pour un millésime donné, l'activité β-glucosidase varie selon la variété. Les activités les plus élevées ont été rencontrées dans les Muscats, le Carignan, la Syrah et le Merlot. Elles sont environ 2,8 fois plus élevées que les activités les plus faibles. Pour une variété donnée, les niveaux d'activité varient fréquemment selon le millésime.</p><p style="text-align: justify;">+++</p><p style="text-align: justify;">β-glucosidase activity in grape was studied. A method of extraction of the enzyme from plant material was optimized and glucosidase activity measured spectrophotometrically using paranitrophenylglucopyranoside as substrate. High concentrations of β-glucosidase were found in grape berry solids (skin and pulp) and low concentrations in the juice. This distribution is similar to that of free terpenols in the same parts of the berry. The β-glucosidase content were very high in grape leaf blades and low in stems. Activity of the enzyme increased during maturation of the fruit. It was found in mature fruit of both aromatic (Muscat of Alexandria, Muscat of Frontignan, Muscat of Hamburg) and non-aromatic (Carignane, Grenache, Cinsaut, Baroque, Cabernet-Sauvignon, Sirah, Merlot) varieties. β-glucosidase activity varied according to variety for a given vintage. The highest activities (approximately 2.8 times higher than the lowest observed) were found in the differents Muscats and also in non-aromatic varieties such as Sirah, Merlot and Carignane. β-glucosidase activity in a given variety was frequently found to vary considerably from one vintage to another.</p>

A carrier-mediated system for transport of biotin in rat intestine in vitro

1987 ◽  
Vol 252 (1) ◽  
pp. G52-G55 ◽  
Author(s):  
H. M. Said ◽  
R. Redha
Keyword(s):  
Methyl Ester ◽  
Temperature Dependent ◽  
Rat Intestine ◽  
Simple Diffusion ◽  
Low Concentrations ◽  
Structural Analogues ◽  
High Concentrations ◽  
Biotin Molecule ◽  
Energy Dependent

Transport of biotin was examined in rat intestine using the everted sac technique. Transport of 0.1 microM biotin was linear with time for at least 30 min of incubation and occurred at a rate of 3.7 pmol X g initial tissue wet wt-1 X min-1. Transport of biotin was higher in the jejunum than the ileum and was minimum in the colon (85 +/- 6, 36 +/- 6, and 2.8 +/- 0.6 pmol X g initial tissue wet wt-1 X 25 min-1, respectively). In the jejunum, transport of biotin was saturable at low concentrations (Kt = 3.73, microM, Vmax = 3.11 nmol X g initial tissue wet wt-1 X 25 min-1) but linear at higher concentrations (greater than 10 microM). The transport of low concentrations of biotin was inhibited by structural analogues (desthiobiotin, biotin methyl ester, diaminobiotin, and biocytin), Na+ dependent, energy dependent, temperature dependent, and proceeded against a concentration gradient in the serosal compartment. No metabolic alteration occurs to the biotin molecule during transport. This study demonstrates that biotin transport in rat intestine occurs by a carrier-mediated process at low concentrations and by simple diffusion at high concentrations. Furthermore, the carrier-mediated process is Na+, energy, and temperature dependent.

Mitotic blocking agents for suspension cultures of maize 'Black Mexican Sweet' cell lines

Genome ◽  
1989 ◽  
Vol 32 (3) ◽  
pp. 475-478 ◽  
Author(s):  
J. Stadler ◽  
R. Phillips ◽  
M. Leonard
Keyword(s):  
Mitotic Index ◽  
Culture Medium ◽  
Colchicine Treatment ◽  
Mitotic Arrest ◽  
Suspension Cultures ◽  
Metaphase Arrest ◽  
Low Concentrations ◽  
High Concentrations ◽  
Very High ◽  
Black Mexican Sweet

Good metaphase arrest (25% mitotic index) in maize (Zea mays L.) 'Black Mexican Sweet' suspension cultures can be obtained with colchicine treatment alone, but only if very high concentrations (0.5%; 12.5 mM) are used. This colchicine concentration is 5- to 10-fold greater than that required for optimum mitotic arrest in cell cultures of other plant species. In contrast, we report that the herbicide amiprophos methyl (APM) is a much more efficient metaphase inhibitor for 'Black Mexican Sweet' suspension cultures than colchicine. Low concentrations (50 μm) of APM applied for 21–28 h produce a similar 25% mitotic index, and the growth-inhibiting effects of this treatment are undetectable 24 h after the removal of APM from the culture medium, APM, therefore, may be a useful agent for mitotic arrest in experiments which require survival of the treated cells. Another antitubulin herbicide, trifuralin, also was tested for ability to promote metaphase arrest in 'Black Mexican Sweet' cultures, but it proved to be ineffective.Key words: mitotic arrest, colchicine, phosphoric amide herbicide.

Yeast actin with a subdomain 4 mutation (A204C) exhibits increased pointed-end critical concentration

2007 ◽  
Vol 85 (3) ◽  
pp. 319-325 ◽  
Author(s):  
David J. Teal ◽  
John F. Dawson
Keyword(s):  
Actin Polymerization ◽  
Critical Concentration ◽  
Structural Studies ◽  
Wild Type ◽  
Low Concentrations ◽  
Engineering Strategy ◽  
High Concentrations ◽  
Pointed End ◽  
Very High

Characterizing mutants of actin that do not polymerize will advance our understanding of the mechanism of actin polymerization and will be invaluable for the production of short F-actin structures for structural studies. To circumvent the problem of expressing dominant lethal nonpolymerizing actin in yeast, we adopted a cysteine engineering strategy. Here we report the characterization of a mutant of yeast actin, AC-actin, possessing a single pointed-end mutation, A204C. Expression of this mutant in yeast results in actin-polymerization-deficient phenotypes. When copolymerized with wild-type actin, ATP–AC-actin is incorporated into filaments. ADP–AC-actin participates in the nucleation and elongation of wild-type filaments only at very high concentrations. At low concentrations, ADP–AC-actin appears to participate only in the nucleation of wild-type filaments, suggesting that Ala-204 is involved in modulating the critical concentration of the pointed end of actin.

Hormone-stimulated glycogenolysis in isolated goldfish hepatocytes

1976 ◽  
Vol 231 (1) ◽  
pp. 191-197 ◽  
Author(s):  
MJ Birnbaum ◽  
J Schultz ◽  
JN Fain
Keyword(s):  
Cyclic Amp ◽  
Blocking Agent ◽  
Ionophore A23187 ◽  
Bacterial Collagenase ◽  
Goldfish Carassius Auratus ◽  
Low Concentrations ◽  
Cyclic Amp Accumulation ◽  
The Common ◽  
High Concentrations ◽  
Very High

Hepatocytes isolated from the liver of the common goldfish Carassius auratus L. with crude bacterial collagenase maintained ATP levels for at least 2 h. Glycogenolysis was maximally activated by 1 X 10(-6) M epinephrine and 5.8 X 10(-9) M glucagon. In liver cells incubated in calcium-free buffer containing 1 mM ethylene glycol-bis-(beta-aminoethylether)-N,N'-tetraacetic acid, basal glycogenolysis was enhanced by the addition of 1-4 mM calcium but the elevation of cyclic AMP and glycogenolysis due to epinephrine was unaffected by calcium. The divalent cation ionophore A23187 did not alter basal or hormone-stimulated glycogenolysis. Isoproterenol was approximately as potent as epinephrine but phenylephrine was glycogenolytic only at very high concentrations. l-Propranolol competitively inhibited the increased glycogenolysis due to catecholamines but phentolamine was ineffective as a blocking agent. Isoproterenol and epinephrine stimulated glycogenolysis at lower concentrations than those required to elevate cyclic AMP accumulation. Phenylephrine was without effect on cyclic AMP. Propranolol competitively inhibited both epinephrine- and isoproterenol-stimulated cyclic AMP accumulation, but phentolamine did not block either response. Catecholamine-stimulated glycogenolysis in goldfish liver is apparently a beta-adrenergic effect. However, low concentrations of epinephrine enhance glycogenolysis without affecting total cyclic AMP.

scholarly journals Some properties of pyruvate and 2-oxoglutarate oxidation by blowfly flight-muscle mitochondria

1972 ◽  
Vol 127 (1) ◽  
pp. 271-283 ◽  
Author(s):  
R. G. Hansford
Keyword(s):  
Oxygen Uptake ◽  
Isocitrate Dehydrogenase ◽  
Adenine Nucleotides ◽  
Slight Reduction ◽  
Glycerol Phosphate ◽  
Pyruvate Oxidation ◽  
Low Concentrations ◽  
High Concentrations ◽  
Kinetics Of ◽  
Very High

1. High rates of state 3 pyruvate oxidation are dependent on high concentrations of inorganic phosphate and a predominance of ADP in the intramitochondrial pool of adenine nucleotides. The latter requirement is most marked at alkaline pH values, where ATP is profoundly inhibitory. 2. Addition of CaCl2 during state 4, state 3 (Chance & Williams, 1955) or uncoupled pyruvate oxidation causes a marked inhibition in the rate of oxygen uptake when low concentrations of mitochondria are employed, but may lead to an enhancement of state 4 oxygen uptake when very high concentrations of mitochondria are used. 3. These properties are consistent with the kinetics of the NAD-linked isocitrate dehydrogenase (EC 1.1.1.41) from this tissue, which is activated by isocitrate, citrate, ADP, phosphate and H+ ions, and inhibited by ATP, NADH and Ca2+. 4. Studies of the redox state of NAD and cytochrome c show that addition of ADP during pyruvate oxidation causes a slight reduction, whereas addition during glycerol phosphate oxidation causes a `classical' oxidation. Nevertheless, it is concluded that pyruvate oxidation is probably limited by the respiratory chain in state 4 and by the NAD-linked isocitrate dehydrogenase in state 3. 5. The oxidation of 2-oxoglutarate by swollen mitochondria is also stimulated by high concentrations of ADP and phosphate, and is not uncoupled by arsenate.

scholarly journals Wheat-germ aspartate transcarbamoylase. The effect of ligands on the inactivation of the enzyme by trypsin and denaturing agents

1973 ◽  
Vol 131 (4) ◽  
pp. 699-706 ◽  
Author(s):  
Robert J. Yon
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Wheat Germ ◽  
Sodium Dodecyl ◽  
Aspartate Transcarbamoylase ◽  
Carbamoyl Phosphate ◽  
Low Concentrations ◽  
Alkaline Conditions ◽  
High Concentrations ◽  
Very High ◽  
Resistant State

In the absence of added ligands aspartate transcarbamoylase (EC 2.1.3.2) from wheat germ is inactivated fairly rapidly by trypsin, by heat (60°C), by highly alkaline conditions (pH11.3) and by sodium dodecyl sulphate. Addition of UMP alone, at low concentrations, decreases the rate of inactivation by each of these agents significantly. Carbamoyl phosphate alone does not alter the rate of inactivation by trypsin and by the detergent, but it antagonizes the effect of UMP in protecting the enzyme against these agents. These results have been interpreted to mean that two conformational states are reversibly accessible to the enzyme, namely an easily inactivated state favoured in the presence of carbamoyl phosphate and a more resistant state favoured in the presence of UMP. In the absence of ligands the enzyme is in the easily inactivated conformation. At very high concentrations l-aspartate also protects the enzyme but to a smaller extent than UMP. Some implications of these results are discussed.

Characteristics of spermidine uptake by isolated rat enterocytes

1989 ◽  
Vol 256 (5) ◽  
pp. G905-G910 ◽  
Author(s):  
J. Kumagai ◽  
R. Jain ◽  
L. R. Johnson
Keyword(s):  
Temperature Dependent ◽  
New Synthesis ◽  
Low Concentrations ◽  
Carrier Mechanism ◽  
Electrical Gradient ◽  
High Concentrations ◽  
The One ◽  
Energy Dependent ◽  
Rat Enterocytes ◽  
Isolated Rat

Eukaryotic cells require polyamines for growth. The supply of polyamines to growing cells may be increased either by new synthesis or increased uptake. We have recently shown that putrescine uptake by isolated rat enterocytes is energy dependent, saturable, and ouabain insensitive. Although putrescine uptake was inhibited by putrescine and cadaverine, it was not inhibited by equal concentrations of spermine and spermidine. These data indicated that a carrier mechanism separate from that putrescine existed for spermidine and spermine. In the current study spermidine uptake by isolated enterocytes was saturable, temperature dependent, and inhibited by 1 mM KCN. Kinetic analysis resulted in a Km = 2.51 x 10(-6) M and a Vmax = 3.57 x 10(-12) mol.10(6) cells-1.15 min-1. Spermidine uptake was 70% inhibited by 1 mM ouabain. Replacement of sodium by choline, lithium, tetramethylammonium, or N-methyl-D-glucamine also inhibited spermidine uptake. Replacement of Na+ by mannitol or sucrose, however, depressed uptake but not significantly. Spermidine uptake was inhibited by 1 mM ouabain. Spermidine uptake was inhibited by relatively low concentrations of spermine and high concentrations of putrescine; while putrescine uptake was inhibited by relatively high concentrations of both spermine and spermidine. Kinetic data indicated that spermidine and spermine share a carrier that is distinct from the one mediating the uptake of putrescine. While spermidine uptake does not appear to depend on Na+ cotransport, it may be dependent on the electrical gradient established by the Na+-K+-ATPase.

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