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  • Springer  (16)
  • Periodicals Archive Online (PAO)  (1)
  • 1985-1989
  • 1975-1979  (17)
  • 1978  (17)
  • 1
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
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    Ithaca, N.Y. : Periodicals Archive Online (PAO)
    Industrial and Labor Relations Review. 31:2 (1978:Jan.) 205 
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  • 3
    ISSN: 1432-0827
    Keywords: Nerve growth factor ; Bone resorption ; Parathyroid hormone ; Insulin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The effects of 7S nerve growth factor (NGF) and its isolated α, β, and γ subunits on bone resorption were assessed in a tissue culture system in which the degree of resorption was determined by measuring the release of45Ca from prelabeled fetal rat radii and ulnae. It was found that 7S-NGF, through the activity of its γ, subunit, inhibits parathyroid hormone (PTH)-stimulated but not-unstimulated bone resorption. The following observations suggest that γ-NGF, a trypsin-like molecule, blocks PTH-induced bone resorption by enzymatic degradation of PTH: (a) γ-NGF does not inhibit bone resorption stimulated by the steroid, 1,25-dihydroxycholecalciferol; (b) trypsin is as effective as γ-NGF in inhibiting PTH-stimulated bone resorption; (c) the PTH-inhibitory action of both γ-NGF and trypsin are eliminated by inactivating these enzymes with diisopropyl fluorophosphate; and (d) addition of γ-NGF to the cultures 2 days after the inclusion of PTH does not result in inhibition of bone resorption. Similarly, when the subunit is added to the culture medium before the hormone, there is no inhibition of resorption. The latter observation suggests that the target of γ-NGF is the PTH molecule rather than its membrane receptors. Crystalline bovine insulin inhibits the γ-NGF suppression of PTH-induced bone resorption. This effect, however, is not mimicked by the addition of zinc, which is present in commerical insulin preparations, to the culture medium. Consequently, insulin must inhibit NGF by some mechanism other than the influence of zinc.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 25 (1978), S. 233-240 
    ISSN: 1432-0827
    Keywords: Bone ; Bone resorption ; Albumin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary A fraction (brA), which causes resorption of fetal rat bones in vitro, has been concentrated from bovine serum albumin by anion exchange column chromatography on DEAE Sephadex. This active fraction has also been prepared using DEAE Sephadex A-50 by a batch method with a 0.09M NaCl, 0.1M TRIS buffer, pH 8.35. BrA was 10–30 times more potent than the original albumin. The retained material, which constitutes the bulk of the protein and has less activity than the original albumin, elutes with 0.45M NaCl. Similar treatment of serumα,β or γ globulins does not yield brA. Further enhancement of the bone resorbing activity of brA can be obtained with (NH4)2SO4 fractionation or extraction with CH3OH∶CHCl3. Heating at 55° C for 2 h or at 100° C for 10 min does not affect the activity; overnight incubation with protease destroys the bone resorbing effect. The bone resorbing activity is not removed by dialysis and does not correlate with the protease activity of the fraction. The action of brA is inhibited by 3 mM PO4, 1 μg/ml calcitonin or glucagon, 10−7 M dexamethasone or 0.02 μg/ml actinomycin D. The bone resorbing activity of brA is partially inhibited by 10−7–10−5 M indomethacin. PTH did not elicit bone resorption when added to cultures incubated in chemically defined medium supplemented with 0.1 mg/ml brA. However, brA did not inhibit PTH-induced resorption.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 25 (1978), S. 85-92 
    ISSN: 1432-0827
    Keywords: Fracture callus cartilage ; Matrix vesicles ; Alkaline phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Extracellular matrix vesicles from fracture callus cartilage were isolated by differential centrifugation and resolved by equilibrium centrifugation on a discontinuous sucrose gradient into two bands. The phosphohydrolytic activity towards p-nitrophenyl phosphate, tetrasodium pyrophosphate and adenosine triphosphate was distributed similarly after differential and equilibrium centrifugation suggesting the association of this activity with the matrix vesicles. The two bands isolated by equilibrium centrifugation of the partially purified vesicular preparation demonstrated high levels of alkaline phosphatase activity. Observed with an electron microscope, the 1.07–1.14 g/cm3 band from the gradient was enriched in electron luscent matrix vesicles while the 1.27 g/cm3 band contained electron dense matrix vesicles. Enzymatic analysis of the 1.27 g/cm3 band indicated a slight contamination due to the presence of mitochondria and lysosomes while the 1.07–1.14 g/cm3 band gave no enzymatic indication of subcellular contamination. A phosphohydrolytic enzyme active towards p-nitrophenyl phosphate, tetrasodium pyrophosphate and adenosine triphosphate was purified from the 1.07–1.14 g/cm3 fraction by DEAE-cellulose column chromatography. Electron micrographs of callus cartilage sections demonstrated densification of the plasma membrane and matrix vesicles following substrate incubation withβ-glycerophosphate or tetrasodium pyrophosphate. The histochemical and biochemical data indicate that a phosphatase, with multiple substrate specificity, is a component of fracture callus cartilage matrix vesicles.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Two new deficient glucose-phosphate-isomerase (GPI) variants have been described in patients suffering from severe chronic hemolytic anemias. The patients' parents were consanguineous, such that the patients were true homozygotes for the mutated GPI genes. In both cases the main cause of the defect in enzyme activity was molecular instability of the mutated GPI molecules, their catalytic activity being nearly normal. GPI ‘Paris’ was characterized by a slow electrophoretic migration and, above all, a drastically altered affinity for the substrates glucose-6-phosphate (decreased) and fructose-6-phosphate (increased). GPI “Enfants malades’ exhibited a slightly reduced electrophoretic mobility, an abnormal curve of the activity in function of pH, and an abnormal ratio of maximal velocity in the backward direction (fructose-6-phosphate»glucose-6-phosphate) to that in the forward direction (glucose-6-phosphate»fructose-6-phosphate). No clear relation could be proved between the kinetic abnormalities of the mutant GPI variants on the one hand and the metabolic changes of the GPI-deficient red cells and the severity of hemolysis on the other. Finally we emphasized the possible role of the impairment of hexosemonophosphate pathway in the reduction of viability of the GPI-deficient red cells.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Erythrocyte pyruvate kinase (PK) deficiency was detected in a boy of dutch origin. Immunologic, electrophoretic, and kinetic studies of the enzymes of propositus and the members of his family demonstrated that the boy was heterozygote for two different mutant PK alleles. The mutant enzyme, for which his mother was heterozygote, was characterized by a lower immunologic specific activity, a decreased affinity for the substrate phospho-enol-pyruvate, and a loss of homotropic interactions toward this substrate, an increased affinity toward the allosteric inhibitor MgATP2-, a decreased affinity for the activator fructose-1,6-diphosphate, and a lowered pH optimum. Electrophoresis, Km app. for MgADP, and the reactivity toward the purine nucleotide substrate analogues were normal. The mutant enzyme for which his father was heterozygote was characterized by a decreased affinity for the substrate phospho-enol-pyruvate and a loss of homotropic interactions toward this substrate. All other parameters mentioned above were normal. The use of a kinetic study of mutant enzymes for the detection of heterozygotes is discussed.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A new G6PD variant, called G6PD Vientiane, has been discovered in a patient from Laos. The characteristics of this variant are: mild enzyme deficiency (about 50% of the normal activity) in the granulocytes and the red cells, with normal G6PD-related antigen concentration; increased stability; normal Km glucose 6-phosphate and NADP+; increased inhibition constant by NADPH; decreased inhibition by ATP; slightly increased utilization of the substrate analogue; abnormal pH curve, with maximum activity at pH 9.5; slightly reduced starch gel electrophoretic migration. The implications of the molecular stability of a deficient mutant variant are discussed.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-1009
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 22 (1978), S. 153-158 
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Autoantibodies to the insulin receptor mimic the effects of insulin on glycogen synthase and phosphorylase. The interaction of antibodies with adipocyte cell surface insulin receptors seems sufficient to promote stable changes in the activities of these intracellular enzymes, suggesting that internalization or processing of insulin is not important in the generation of these biological responses.
    Type of Medium: Electronic Resource
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