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  • Articles  (98)
  • Springer  (98)
  • Public Library of Science (PLoS)
  • Chemistry and Pharmacology  (98)
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  • Articles  (98)
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  • 11
    Electronic Resource
    Electronic Resource
    Identification of the molecular basis for phosphorylase hypersensitivity in cultured diabetic cardiomyocytes (1995)
    Springer
    Molecular and cellular biochemistry 145 (1995), S. 131-139 
    Details
    ISSN: 1573-4919
    Keywords: glycogen phosphorylase ; alloxan-diabetes ; cardiomyocytes ; cGMP ; phosphodiesterase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The focus of this study was to identify the molecular basis for the hypersensitive response of glycogen phosphorylase activation to epinephrine stimulation in alloxan diabetic-derived cardiomyocytes. Cyclic AMP levels were found not to be significantly different between normal and diabetic-derived cells while cGMP concentrations were found consistently to be significantly lower in diabetic-derived cells than in normal cells. Treatment with cyclic GMP analogues did not affect phosphorylase activation by epinephrine in normal cardiomyocytes whereas, IBMX, a nonselective phosphodiesterase inhibitor, had a significant effect on basal and agonist-stimulated phosphorylase activity in both normal and diabetic-derived cardiomyocytes. Differences in the time course for the rate of decay of phosphorylasea from agonist-stimulated to basal levels were observed between normal and diabetic cells. After 3 h in primary culture, phosphorylasea activity returned to basal levels more quickly in normal than in diabetic-derived cells while after 24 h in culture, the time for phosphorylasea decay was not significantly different between normal and diabetic myocytes and was longer than the 3 h response. After 3 h in primary culture, no significant difference in phosphorylase kinase activity was observed between normal and diabetic-derived cells exposed to epinephrine whereas, after 24 h in culture, phosphorylase kinase activity was significantly decreased in diabetic cells under basal and agonist-stimulated conditions. These data collectively suggest that the hypersensitive response of glycogen phosphorylase to epinephrine stimulation in diabetic-derived cardiomyocytes is not due to a defect present at the level of phosphorylase kinase but may, in part, result from an alteration in cardiac phosphodiesterase activity resulting from diminished intracellular cyclic GMP concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00935485
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  • 12
    Electronic Resource
    Electronic Resource
    Purification and the immunological characterization of rat protein phosphatase 2A: enzyme levels in diabetic liver and heart (1991)
    Springer
    Molecular and cellular biochemistry 101 (1991), S. 167-174 
    Details
    ISSN: 1573-4919
    Keywords: rat protein phosphatase 2A ; liver ; heart ; diabetes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Protein phosphatase 2A1 was purified from rat skeletal muscle and used to produce antisera to the three subunits of the holoenzyme. Affinity purified antibodies specific for the subunits of the phosphatase enzyme were found to recognize the type 2A1 and 2A2 phosphatase from rat skeletal muscle, heart, liver, brain and erythrocytes and were used to investigate the effects of diabetes on the levels of this enzyme in liver and heart. Phosphorylase phosphatase assays coupled with immunoblot analysis of fractionated rat liver and heart cytosol from normal and diabetic animals show no apparent differences in the quantity or activity of these enzymes following the induction of alloxan diabetes. When considering these results and the normal physiological concentrations of known effectors of these enzymes, it is likely that protein phosphatase 2A1 and 2A2 are not responsible for the dephosphorylation of phosphorylase a under physiological conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00229533
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  • 13
    Electronic Resource
    Electronic Resource
    The third leg: Molecular dynamics simulations of lipid binding proteins (1999)
    Springer
    Molecular and cellular biochemistry 192 (1999), S. 143-156 
    Details
    ISSN: 1573-4919
    Keywords: molecular dynamics ; LBP ; FABP ; structure-function ; protein-lipid interactions ; rational drug design
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Molecular dynamics computer simulations can provide a third leg which balances the contributions of both structural biology and binding studies performed on the lipid binding protein family. In this context, these calculations help to establish a dialogue between all three communities, by relating experimental observables with details of structure. Working towards this connection is important, since experience has shown the difficulty of inferring thermodynamic properties from a single static conformation. The challenge is exemplified by ongoing attempts to interpret the impact of mutagenesis on structure and function (i.e. binding). A detailed atomic-level understanding of this system could be achieved with the support of all three legs, paving the way towards rational design of proteins with novel specificities. This paper provides an outline of the connections possible between experiment and theory concerning lipid binding proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006818203334
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  • 14
    Electronic Resource
    Electronic Resource
    Control of lysosomal acid phosphatase expression in man-mouse cell hybrids (1974)
    Springer
    Biochemical genetics 11 (1974), S. 121-139 
    Details
    ISSN: 1573-4927
    Keywords: gene expression ; gene mapping ; lysosomal enzymes ; cell fusion ; gel electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Lysosomal acid phosphatase activity in human and mouse cells was separated into multiple zones by starch gel electrophoresis. One of the two major zones in the mouse was apparently extinguished when genetic information from man and the mouse was combined in proliferating man-mouse somatic cell hybrids. The evidence suggested that the absence of the mouse lysosomal acid phosphatase (mAP-1) was influenced by the human genome. The gene coding for human acid phosphatase (hAP-1) was shown to be unlinked to the presumed human component which extinguished the mouse acid phosphatase (mAP-1). The mechanism of “extinction” is postulated to be a modification in the processing of the mouse lysosomal enzyme. A dimeric structure was suggested for acid phosphatase-1 of man, mouse, and rat since a single hybrid enzyme was expressed in man-mouse and mouse-rat somatic cell hybrids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485769
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  • 15
    Electronic Resource
    Electronic Resource
    The amino acid substitution and some chemical properties of a variant human erythrocyte carbonic anhydrase: Carbonic anhydrase IdMichigan (1967)
    Springer
    Biochemical genetics 1 (1967), S. 171-195 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Carbonic anhydrase IdMichigan, an electrophoretic variant of human red cell carbonic anhydrase I, was purified from erythrocytes obtained from an individual heterozygous for the trait. Primary structural analysis indicates that a lysine residue has exchanged for a threonine residue in the variant enzyme. After isolation, there was approximately 1.8 times as much normal as variant enzyme. Thermostability studies demonstrated that carbonic anhydrase Id was more thermolabile than the normal enzyme. The normal and variant enzymes showed no differences in specific carboxylesterase activity or CO2 hydratase activity. Utilizing the carboxylesterase activity toward β-naphthyl acetate, the normal and variant enzymes had similar Michaelis constants, pH profiles, and rates of inhibition by acetazolamide. Immunochemical studies did not demonstrate an antigenic difference for the variant enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486517
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  • 16
    Electronic Resource
    Electronic Resource
    Biochemical polymorphisms in feral and inbred mice (Mus musculus) (1971)
    Springer
    Biochemical genetics 5 (1971), S. 457-466 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Examination of the frequencies of several loci controlling isozymes in three geographically distinct feral populations of mice showed the average animal to be heterozygous at 10.3% of his loci. There was no evidence for interaction between loci, nor any evidence for inbreeding in the populations. Thirty-nine inbred strains, including four newly derived ones, were also characterized for their alleles for as many as 16 polymorphic loci. Among these strains, variability is at least as great as in any single feral population, but probably less than that found among all feral populations of the species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00487135
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  • 17
    Electronic Resource
    Electronic Resource
    Phosphoglucomutase electrophoretic variants in the mouse (1969)
    Springer
    Biochemical genetics 3 (1969), S. 25-35 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The phosphoglucomutase (PGM) electrophoretic phenotype of the mouse (Mus musculus) consists of several distinct components which can be grouped into two major zones designated PGM-1 and PGM-2. Evidence presented here indicates that each zone is controlled by a single genetic locus denoted Pgm-1 and Pgm-2, respectively. Two variant forms segregated at the Pgm-1 locus. They were codominantly expressed and inherited as alleles at an autosomal locus. The alleles were termed Pgm-1 a (fast) and Pgm-1 b (slow). These alleles were separately fixed in a number of inbred strains of mice. Preliminary evidence based on wild mouse phenotypes indicates that variant forms also exist for PGM-2 which are inherited as alleles at an autosomal locus. Genetic linkage relationships have not been determined for these loci. PGM-1 variants and PGM-2 were expressed in mouse fibroblasts in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485972
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  • 18
    Electronic Resource
    Electronic Resource
    Analysis of the loop-helix interaction in bundle motif protein structures (1995)
    Springer
    The protein journal 14 (1995), S. 559-566 
    Details
    ISSN: 1573-4943
    Keywords: Bovine somatotropin ; methemerythrin ; cytochrome b-562 ; cytochrome c′ ; CHARMM ; GROMOS ; UHBD
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Molecular dynamics simulations and energy analysis have been carried out to study the structural mobility and stability of the four α-helix bundle motifs. The simulation results as well as the X-ray data show that the atomic RMS fluctuation is larger at the loop region for four representative proteins investigated: methemerythrin, cytochrome b-562, cytochrome c′, and bovine somatotropin. The loop-loop, helix-helix, and loop-helix interactions are computed for the unfolded and folded proteins. In the folded and solvated protein structures the loop-helix interaction is stronger than the helix-helix interaction, especially in the electrostatic component. But the stabilization energies of both the loop-helix and the helix-helix interactions relative to the those of an unfolded structure are of the same order of magnitude. The stabilization due to protein-solvent interaction is greater in the helix region than in the loop region. The percentage of hydrophilic solvent accessible area for the four proteins studied was calculated with the method of Eisenberg and McLachlan. The percentage of the hydrophilic area is greater in the loops than in the helices. A Poisson-Boltzmann calculation shows that the potential from the loops acting on a helix is generally more negative than that from other helices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886882
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  • 19
    Electronic Resource
    Electronic Resource
    Preparation of a human lung purified plasma membrane fraction: Confirmation by enzyme markers, electron microscopy, and histamine H1 receptor binding (1984)
    Springer
    The journal of membrane biology 79 (1984), S. 33-39 
    Details
    ISSN: 1432-1424
    Keywords: plasma membrane ; lung ; histamine receptors ; 5′ nucleotidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary A simple and rapid method of isolating plasma membranes from human peripheral lung tissue is described. The method involves homogenization of tissue in 0.25m sucrose-buffered medium followed by differential and sucrose density gradient centrifugation. Enzymatic and morphological characterization of the plasma membrane fraction revealed minimal contamination by nonplasma membrane fragments. The isolated plasma membranes showed an 18-fold purification of 5′-nucleotidase activity compared to the original homogenate. Electronmicroscopic studies of the plasma membrane fraction revealed the presence of small membrane vesicles having a trilaminar membrane structure. To further examine the purity of the plasma membrane preparation, the binding of the H1 receptor antagonist,3H pyrilamine, to the plasma membrane-enriched fraction was compared to the binding to crude membrane preparations. Both the plasma membrane-enriched fraction and the crude membrane preparation had similar Kd's for the histamine antagonist, but the plasma membrane-enriched fraction had a threefold greater binding capacity, reflecting the relative enrichment of plasma membranes of the preparation. Thus, a method has been developed for the isolation of plasma membranes from human peripheral lung which should provide material for a variety of biochemical and pharmacological studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868524
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  • 20
    Electronic Resource
    Electronic Resource
    Classification of electrode glasses including structural parameters (1994)
    Springer
    Fresenius' Zeitschrift für analytische Chemie 349 (1994), S. 257-258 
    Details
    ISSN: 1618-2650
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Cluster Analysis has been shown to be partially suitable for the classification of glasses. The expansion of the clusters on the Seger's diagram allows an investigation of the influence of the different glass components. Variation of the SiO2 content results in a smaller change of properties than variation of the Na2O/RO relationship. Principal Component Analysis is convenient for showing correlations between the composition of the examined glasses, the glass structure parameters, and the different electrode properties.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00323307
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