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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Inorganic chemistry 6 (1967), S. 318-320 
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Inorganic chemistry 16 (1977), S. 486-488 
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Inorganic chemistry 18 (1979), S. 1808-1811 
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 5 (1969), S. 192-194 
    ISSN: 1432-0428
    Keywords: Insulin antibodies ; dose ; total binding capacity ; preferential binding ; beef/pork insulin anti-bodies
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Résumé Les auteurs ont effectué une étude de deux groupes de sérums de diabétiques, en ce qui concerne la capacité totale de liaison à l'insuline et la liaison préférentielle avec l'insuline de boeuf et de porc. Le groupe I (25 patients) a reçu principalement de l'insuline de boeuf, avec un rapport boeuf/porc d'environ 3∶1; le groupe II (13 patients) a reçu de l'insuline contenant au moins 97% d'insuline de porc. Dans le groupe I la capacité moyenne de liaison avec l'insuline était de 15.38 U/litre, et dans 21 cas l'insuline de boeuf était liée de façon préférentielle par rapport à l'insuline de porc. Le groupe II a été divisé en deux sous-groupes: le groupe IIa (7 patients) dont les sérums liaient plus l'insuline de boeuf que celle de porc, la capacité moyenne de liaison avec l'insuline était de 8 U/l. Le groupe IIb (6 patients) dont les sérums liaient l'insuline de porc mieux que celle de boeuf, ou ne montraient pas de préférence, la capacité moyenne de liaison avec l'insuline était de 3.1 U/l. La dose moyenne d'insuline dans le groupe IIa était de 34.8 et dans le groupe IIb, elle était de 24. La capacité moyenne de liaison avec l'insuline et la dose moyenne d'insuline étaient significativement différentes (p 〈 0.05) entre le groupe IIa et le groupe IIb. L'importance éventuelle de ces résultats est discutée.
    Abstract: Zusammenfassung Bei den Seren von 2 Gruppen insulinbehandelter Diabetiker wurde die totale Bindungskapazität für Rinder-und Schweineinsulin bestimmt. Die Patienten aus Gruppe 1 (25 Personen) waren mit einem Mischinsulin behandelt worden, das Rinder-und Schweine-insulin im Verhältnis von 3∶1 enthielt. Die Patienten aus Gruppe 2 (13 Personen) wurden mit nahezu reinem Schweineinsulin (97%) behandelt. Die Insulinbindungskapazität betrug in Gruppe 1 durchschnittlich 15.38 E/l. In 21 Fällen wurde Rinderinsulin stärker als Schweine-insulin gebunden. — Die Patienten aus Gruppe 2 wurden in 2 Untergruppen aufgeteilt: In Gruppe 2a (7 Patienten) zeigte das Serum durchschnittlich eine Insulinbindungskapazität von 8 E/l, Rinderinsulin wurde stärker gebunden als Schweineinsulin. Gruppe 2b bestand aus 6 Patienten. Die mittlere Insulinbindungskapazität betrug 3.1 E/l, die Seren zeigten entweder eine stärkere Bindungsfähigkeit für Schweine-Insulin, oder keine Bevorzugung einer Insulinart. Die mittlere Insulintagesdosis betrug in Gruppe 2a 34.8 und in Gruppe 2b 24 E. Ein Vergleich der Werte für die mittlere Insulinbindungskapazität und die mittlere Insulindosis der Gruppen 2a und 2b zeigte einen statistisch gesicherten Unterschied. Die Ergebnisse werden diskutiert.
    Notes: Summary A study of two groups of diabetic sera has been carried out with reference to total insulin binding capacity and preferential binding of beef and pork insulin. Group I (25 patients) received insulin containing pre-dominantly beef insulin with a beef/pork ratio of 3∶1 approximately; Group II (13 patients) received insulin containing at least 97% pork insulin. In Group I the mean total insulin binding capacity was 15.38U/litre and in 21 beef insulin was preferentially bound with reference to pork insulin. Group II was divided into two subgroups: group IIa, 7 patients, the sera bound beef 〉 pork, and the mean insulin binding capacity was 8 U/l. Group IIb, 6 patients, the sera bound pork 〉 beef or showed no preference, and the mean insulin binding capacity was 3.1 U/l. The mean insulin dose in Group IIa was 34.8 and in Group IIb was 24. The mean insulin binding capacity and mean insulin dose were significantly different (P 〈 0.05) between Group IIa and Group IIb. The possible significance of the results is discussed.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 37 (1994), S. 358-364 
    ISSN: 1432-0428
    Keywords: Key words Protein metabolism, exercise, leucine, hyperglycaemia, ketones.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined whether the increased rates of protein catabolism (proteolysis and leucine oxidation) associated with moderate insulinopenia in subjects with IDDM would be accentuated by prior bicycle exercise (53 % VO2max for 82 min). Insulin infusions maintained plasma glucose concentrations on one study day in “tight” control (TC: 6 mmol/l) and on a separate day in “loose” control (LC: 12 mmol/l). Elevations in serum ketone body, plasma NEFA, and whole-blood branched-chain amino acid concentrations on the loose control day during the basal period persisted throughout the post-exercise recovery period. Amino acid kinetics were estimated during a primed, constant infusion of L-[1-13C]leucine from plasma dilution of α-[1-13C]KIC and expired air 13CO2 enrichments. Loose control was associated with increased rates of whole-body leucine oxidation (LC 25±7 vs TC 21±8 µmol·kg−1·h−1) and protein degradation (LC 127±12 vs TC 118±18 µmol·kg−1·h−1) (both p〈0.05). During the 2-h post exercise recovery period, there were significant decreases in rates of leucine oxidation (LC 21±7, TC 16±7) and protein degradation (LC 112±13, TC 107±11), compared to the basal period (both p〈0.05, basal vs recovery). Rates of whole-body protein synthesis were unchanged by prior exercise. In conclusion, moderate insulinopenia is associated with significantly higher rates of protein degradation and leucine oxidation in the basal state. Following exercise, net protein catabolism is diminished due to reduced rates of protein degradation in the presence of maintained rates of protein synthesis. The significantly increased concentrations of fat-derived substrates (ketone bodies, NEFA) may have prevented the predicted increases in protein catabolism which we anticipated would follow acute exercise during periods of relative insulin deficiency. [Diabetologia (1994) 37: 358–364]
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 37 (1994), S. 358-364 
    ISSN: 1432-0428
    Keywords: Protein metabolism ; exercise ; leucine ; hyperglycaemia ; ketones
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined whether the increased rates of protein catabolism (proteolysis and leucine oxidation) associated with moderate insulinopenia in subjects with IDDM would be accentuated by prior bicycle exercise (53% VO2max for 82 min). Insulin infusions maintained plasma glucose concentrations on one study day in “tight” control (TC: 6 mmol/l) and on a separate day in “loose” control (LC: 12 mmol/l). Elevations in serum ketone body, plasma NEFA, and whole-blood branched-chain amino acid concentrations on the loose control day during the basal period persisted throughout the post-exercise recovery period. Amino acid kinetics were estimated during a primed, constant infusion of l-[1-13C]leucine from plasma dilution of α-[1-13C]KIC and expired air 13CO2 enrichments. Loose control was associated with increased rates of whole-body leucine oxidation (LC 25±7 vs TC 21±8 μmol · kg−1 · h−1) and protein degradation (LC 127±12 vs TC 118±18 μmol · kg−1 · h−1) (both p〈0.05). During the 2-h post exercise recovery period, there were significant decreases in rates of leucine oxidation (LC 21±7, TC 16±7) and protein degradation (LC 112±13, TC 107±11), compared to the basal period (both p〈0.05, basal vs recovery). Rates of wholebody protein synthesis were unchanged by prior exercise. In conclusion, moderate insulinopenia is associated with significantly higher rates of protein degradation and leucine oxidation in the basal state. Following exercise, net protein catabolism is diminished due to reduced rates of protein degradation in the presence of maintained rates of protein synthesis. The significantly increased concentrations of fat-derived substrates (ketone bodies, NEFA) may have prevented the predicted increases in protein catabolism which we anticipated would follow acute exercise during periods of relative insulin deficiency.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. When DNA topoisomerase II (topo II) activity is inhibited with a non-DNA-damaging topo II inhibitor (ICRF-193), mammalian cells become checkpoint arrested in G2-phase. In this study, we analyzed chromosome structure in cells that bypassed this checkpoint. We observed a novel type of chromosome aberration, which we call Ω-figures. These are entangled chromosome regions that indicate the persistence of catenations between nonhomologous sequences. The number of Ω- figures per cell increased sharply as cells evaded the transient block imposed by the topo II-dependent checkpoint, and the presence of caffeine (a checkpoint-evading agent) potentiated this increase. Thus, the removal of nonreplicative catenations, a process that promotes chromosome individualization in G2, may be monitored by the topo II-dependent checkpoint in mammals.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 94 (1991), S. 812-813 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The intensity of infrared absorption bands, observed for large gas-phase ice I clusters and attributed to OH (or OD) groups dangling at the cluster surfaces, has been used to estimate the average size of ice clusters formed under fairly typical static cell conditions. The assignment of bands at 3692 cm−1 (2425 cm−1) to dangling surface groups has been established as credible by comparison with absorption bands presumably produced by dangling groups at the surfaces of pores in microporous amorphous ice. Using fairly standard assumptions about absorptivities and molecular sizes, an estimated cluster size of 25 nm has been obtained for clusters formed at 280 Torr and 80 K in a gaseous mixture containing a He to H2O ratio of 200.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 88 (1988), S. 3086-3091 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The photoexcitation of 2-naphthol as a trace impurity in ice results in the injection of excess protons into the ice network. These protons are immobile at temperatures 〈100 K but warming to ∼120 K generates a near steady-state concentration of mobile protons which decays slowly. This behavior confirms the existence of shallow proton traps in ice which, following Kunst and Warman, are presumed to be intrinsic and, most probably, Bjerrum L defects. The quantity of mobile protons at a given temperature, in a pseudoequilibrium with immobile protons bound to the L defects, is controlled by the temperature coefficients of (a) the pseudoequilibrium constant and (b) the L-defect concentration. Since both the L and D defects are immobile below ∼130 K, the L-defect concentration can be taken to be temperature independent. Consequently, the temperature dependence of the rate at which D2O molecules isolated in H2O cubic ice are converted to (HOD)2 units by mobile protons is a direct measure of the binding energy between the excess protons and the L defects. This binding energy has been estimated at 10.0 kcal/mol. At the completion of each kinetic experiment at T〈126 K, the predominant deuterated species is (HOD)2. Such samples are ideal for observation of the ice L-defect activity which is thermally activated by warming to above 130 K. By following the rate of conversion of (HOD)2 to isolated HOD for the range 134 to 150 K, the activation energy for the L-defect formation and mobility has been determined to be 12.2 kcal for cubic ice. This is close to the value of 12.0 kcal previously determined for cubic ice from isotopic exchange rates, but is less than the accepted value for hexagonal ice of 13.1 kcal/mol. Further, the enthalpy change for ice self-ionization has been estimated as 16.8 kcal from a combination of the activation energies for proton transport (9.5 kcal) and L-defect formation (7.8 kcal) with the L-defect–proton binding energy of 10.0 kcal.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 87 (1987), S. 4126-4131 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: There has recently been a substantial increase in information on low-temperature phase transformations of ice and ice-like substances along with a rapid increse in molecular level information on the defect structure and activity of this subset of hydrogen-bonded solids. These data, some quantitative and some qualitative in nature, are examined from the viewpoint that the phase transformation mechanism depends on the availability of mobile orientational defects (Bjerrum L defects) within the new phase. Some of the data that seem particularly apt for establishing any dependence of the phase transformation on the presence of mobile L defects within the new phase, reflect a strong correlation between transformation rates/temperature and the availability of mobile L defects. One possible inference is that the integrity of a growing phase can be maintained only if defects responsible for orientational mobility at the interface can ultimately achieve equilibrium through recombination. The implications of such a dependence on mobile L defects are examined for a variety of systems. For example, one implication is that, at low temperature (〈160 K), the structure I clathrate hydrate of trimethylene oxide (TMO) should grow more rapidly than the structure II hydrate, since structure I hydrates are known to be relatively rich in mobile defects. New data for the clathrate hydrates of TMO are presented that confirm the preferential growth of the structure I hydrate from amorphous deposits containing water and TMO in ratios ranging from 7:1 to 〉17:1.
    Type of Medium: Electronic Resource
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