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  • 1
    Electronic Resource
    Electronic Resource
    Effect of nitridation on magnetic properties of Fe53Pt47 thin film (2002)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 91 (2002), S. 3145-3149 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: The Fe53Pt47 thin films with varying thickness were prepared using dc magnetron sputtering at various substrate temperatures (i.e., from 250 to 600 °C) on to CrMo seeded glass substrates. The powder x-ray diffraction studies reveal that the ordered fct γ2-FePt phase begins to appear starting from the substrate temperature of 250 °C. The estimated ordering parameters show that the films prepared at 300 °C are well ordered and ordering parameters increase slowly as increasing substrate temperatures. On nitridation of the Fe53Pt47 thin films, expansion of the face centered tetragonal crystal lattice along the c axis is observed. The saturation magnetization is decreased with decreasing film thickness. This has been explained mainly on the basis of size and surface effects of nanocrystals in the films including intergranular interactions. Maximum coercivity of 8.7 kOe is observed for the film thickness of 350 nm. The drastic decrease in magnetization with the increase in nitridation time duration has been attributed to the spin pairing effects as a result of electron supply from interstitial nitrogen atoms to the 3d bands of iron atoms. We observed an increase of Hc from 7.8 kOe for non-nitrided Fe53Pt47 film to 10.8 kOe for a 3 h nitrided film. © 2002 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1436301
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  • 2
    Electronic Resource
    Electronic Resource
    Photoaffinity Labeling of Adenylate Cyclase-Linked Serotonin Receptors in Aplysia Neurons (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 49 (1987), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Serotonin stimulated adenylate cyclase in Aplysia neurons with a Kact of 0.7 μM. Under the same conditions, 1 -[2-(4-aminophenyl)ethyl]4-(3-trifluoromethylphenyl)piperazine stimulated adenylate cyclase with a Kactof 20 μM. The azido derivative of this compound, 1-[2-(4-azidophenyl)ethyl]4-(3-trifluoromethylphenyl)piperazine, or of serotonin, (4-amino, 3-nitrophenylazido-serotonin), also stimulated the cyclase in the dark, but with lower efficiency (Kact 〈 10−4M). Irradiation of the membranes in the presence of 100 μM 1-[2-(4-azidophenyl)ethyl]4-(3-trifluoromethylphenyl)piperazine abolished 75% of the cyclase activity stimulated by 5 μM serotonin. Under the same conditions, 100 μM 4-amino, 3-nitrophenylazido-serotonin did not inhibit serotonin-stimulated adenylate cyclase activity. When [3H] 1 -[2-(4-azidophenyl)ethyl]4-(3-trifluoromethylphenyl)piperazine (20 μM) was irradiated with membranes for 5 min at 4°C, a dozen peptides were labeled, as revealed by a fluorogram of sodium dodecyl sulfate-polyacrylamide gels. Among them, the labeling of five polypeptides (molecular weights of 45,000, 55,000, 63,000, 80,000, and 94,000) was protected by the presence of 0.2 mMserotonin during photolysis. These peptides may be related to serotonin receptors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb01000.x
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  • 3
    Electronic Resource
    Electronic Resource
    Dual Effects of Ascorbate on Serotonin and Spiperone Binding in Rat Cortical Membranes (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 41 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Ascorbate-induced lipid peroxidation, as measured by malonyldialdehyde (MDA) production, caused irreversible decreases in Bmax of both [3H]5-HT and [3H]spiperone binding. CaCl2 (4 mM) inhibited ascorbateinduced MDA formation at ascorbate concentrations 〉0.57 mM, but not at ≤0.57 mM. Under the standard assay conditions (5.7 mM ascorbate and 4 mM CaCl2), CaCl2 inhibited the MDA production caused by ascorbate by 88%, and the loss in [3H]5-HT binding by 57%. Ascorbate still decreased [3H]5-HT binding when lipid peroxidation was completely inhibited by EDTA. This additional effect of ascorbate was reversible after washing the membranes. Other reducing agents (dithiothreitol, glutathione, and metabisulfite) also decreased the binding of [3H]serotonin. In contrast, [3H]spiperone binding was not affected by ascorbate in the absence of lipid peroxidation or by other reducing agents. These experiments demonstrate that ascorbate has a dual and differential effect on serotonin binding sites. First, ascorbate-induced lipid peroxidation irreversibly inactivates both [3H]5-HT and [3H]spiperone binding. Second, independent of lipid peroxidation, there is a direct, reversible effect of ascorbate on [3H]serotonin but not on [3H]spiperone binding, which is probably due to the difference in the biochemical nature of the two serotonin binding sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb00842.x
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  • 4
    Electronic Resource
    Electronic Resource
    DETERMINATION OF MONOAMINE OXIDASE IN RAT BRAIN BY ELECTRON SPIN RESONANCE TECHNIQUES (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 26 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —The recent development of spin-labeling techniques has permitted its application to the measurement of the concentration of rat brain mitochondrial monoamine oxidase (MAO) and detection of possible multiple forms of this enzyme. Spin-labeled p-hydroxyamphetamine (SHA) was used as a probe of the active site of the enzyme. The binding of SHA to MAO was monitored by measuring the intensity of the × band ESR spectra obtained with a Varian V-4502 ESR spectrometer. The measured volume of each sample was about 0·02 ml and time required for each measurement was 5 min. In the presence of MAO, a linear relationship was observed between spectral intensity and the concentration of the spin-label in a range of 4 × 10−6m to 10−3m. A plot of the amount of enzyme-inhibitor complex formed against the concentration of SHA suggested the existence of at least three different affinities of SHA to the possible multiple forms of MAO. Measurements made using a constant concentration of the spin-label (3·21 × 10−5m) resulted in a calibration curve with two plateaus when the concentration of the enzyme-inhibitor complex was plotted against the apparent concentration of MAO. These data also suggested that spin-labeled hydroxyamphetamine had distinctly different affinities toward the multiple forms of MAO that were present in the partially purified preparation employed. Measurements made with constant concentrations of SHA and MAO but with varying temperatures (4-56°C) resulted in a curve with two plateaus which also suggested the existence of at least three different binding affinities of the enzyme preparation for the inhibitor. This ESR technique is simple, rapid, accurate and fairly sensitive. It was also applied to the measurement of MAO in human platelets.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb04453.x-i1
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  • 5
    Electronic Resource
    Electronic Resource
    MONOAMINE OXIDASE: From Genes to Behavior (1999)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Neuroscience 22 (1999), S. 197-217 
    Details
    ISSN: 0147-006X
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Notes: Abstract Cloning of MAO (monoamine oxidase) A and B has demonstrated unequivocally that these enzymes are made up of different polypeptides, and our understanding of MAO structure, regulation, and function has been significantly advanced by studies using their cDNA. MAO A and B genes are located on the X-chromosome (Xp11.23) and comprise 15 exons with identical intron-exon organization, which suggests that they are derived from the same ancestral gene. MAO A and B knock-out mice exhibit distinct differences in neurotransmitter metabolism and behavior. MAO A knock-out mice have elevated brain levels of serotonin, norephinephrine, and dopamine and manifest aggressive behavior similar to human males with a deletion of MAO A. In contrast, MAO B knock-out mice do not exhibit aggression and only levels of phenylethylamine are increased. Mice lacking MAO B are resistant to the Parkinsongenic neurotoxin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Both MAO A and B knock-out mice show increased reactivity to stress. These knock-out mice are valuable models for investigating the role of monoamines in psychoses and neurodegenerative and stress-related disorders.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.neuro.22.1.197
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  • 6
    Electronic Resource
    Electronic Resource
    Fermentation production of keratinase from Bacillus licheniformisPWD-1 and a recombinant B. subtilis FDB-29 (1999)
    Springer
    Journal of industrial microbiology and biotechnology 22 (1999), S. 608-616 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: keratinase production; fermentation; Bacillus; recombinant strain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Bacillus licheniformis PWD-1, the parent strain, and B. subtilis FDB-29, a recombinant strain. In both strains, keratinase was induced by proteinaceous media, and repressed by carbohydrates. A seed culture of B. licheniformis PWD-1 at early age, 6–10 h, is crucial to keratinase production during fermentation, but B. subtilis FDB-29 is insensitive to the seed culture age. During the batch fermentation by both strains, the pH changed from 7.0 to 8.5 while the keratinase activity and productivity stayed at high levels. Control of pH, therefore, is not necessary. The temperature for maximum keratinase production is 37°C for both strains, though B. licheniformis is thermophilic and grows best at 50°C. Optimal levels of dissolved oxygen are 10% and 20% for B. licheniformis and B. subtilis respectively. A scale-up procedure using constant temperature at 37°C was adopted for B. subtilis. On the other hand, a temperature-shift procedure by which an 8-h fermentation at 50°C for growth followed by a shift to 37°C for enzyme production was used for B. licheniformis to shorten the fermentation time and increase enzyme productivity. Production of keratinase by B. licheniformis increased by ten-fold following this new procedure. After respective optimization of fermentation conditions, keratinase production by B. licheniformis PWD-1 is approximately 40% higher than that by B. subtilis FDB-29.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900667
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  • 7
    Electronic Resource
    Electronic Resource
    Monoamine oxidase gene transcription in human cell lines: Treatment with psychoactive drugs and ethanol (1996)
    Springer
    Journal of neural transmission 103 (1996), S. 681-692 
    Details
    ISSN: 1435-1463
    Keywords: Alcohol ; growth hormone ; neuroblastoma ; promoter ; reporter gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In the present study transcriptional activities has been measured with different fragments of the 5′-flanking sequence of the human monoamine oxidase (MAO) genes linked to human growth hormone which was used as a reporter gene. SH-SY5Y neuroblastoma cells and 1242 MG glioma cells were compared under basal conditions as well as after treatments with different drugs. Under basal conditions, the relative reporter activities of the different promoter fragments were similar for both cell lines. No changes in promoter activities, were observed when cells were treated with L-deprenyl, lithium chloride or raclopride. In contrast, increases (2–3-fold) in both reporter gene expression and enzyme activity were observed after ethanol treatment of cells transfected with MAO-B fragments. Gel retardation analysis showed that ethanol caused changes in transcription factor binding to the MAO-B core promoter in both the SH-SY5Y and 1242 MG cell lines in a cell-type specific fashion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01271228
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  • 8
    Electronic Resource
    Electronic Resource
    Expression of the Bacillus licheniformis PWD-1 keratinase gene in B. subtilis (1997)
    Springer
    Journal of industrial microbiology and biotechnology 19 (1997), S. 134-138 
    Details
    ISSN: 1476-5535
    Keywords: Keywords: keratinase; gene cloning; gene expression; Bacilli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The kerA gene which encodes the enzyme keratinase was isolated from the feather-degrading bacterium Bacillus licheniformis PWD-1. The entire gene, including pre-, pro- and mature protein regions, was cloned with Pker, its own promoter, P43, the vegetative growth promoter, or the combination of P43-Pker into plasmid pUB18. Transformation of the protease-deficient strain B. subtilis DB104 with these plasmids generated transformant strains FDB-3, FDB-108 and FDB-29 respectively. All transformants expressed active keratinase in both feather and LB media, in contrast to PWD-1, in which kerA was repressed when grown in LB medium. With P43-Pker upstream of kerA, FDB-29 displayed the highest activity in feather medium. Production of keratinase in PWD-1 and transformants was further characterized when glucose or casamino acids were supplemented into the feather medium. These studies help understand the regulation of kerA expression and, in the long run, can help strain development and medium conditioning for the production of this industrially important keratinase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/sj.jim.2900440
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of nickel on biological methane generation from a laboratory poultry waste digesterPaper No. 9143 of the North Carolina Agricultural Research Service, Raleigh, Nc. The use of trade names in this article does not imply endorsement by the N.C. Agricultural Research Service nor criticism of similar ones not mentioned. (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1608-1610 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Nickel added in concentrations as low as 10μM significantly increased biogas production in a laboratory poultry waste digester utilizing excreta from laying hens as the organic energy source. It was shown that the initial rate of biogas production increased as early as 4 h after the addition of nickel to the laboratory cultures. Analysis of the excreta for nickel content prior to addition of exogenous NiCl2 showed appreciable amounts of nickel present. The data indicate that nickel naturally present in layer excreta is suboptimal or unavailable to the bacteria for biogas production purposes.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260281103
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  • 10
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    Cognitive abnormalities in MAO A/B KO mice [Neuroscience] (2013)
    National Academy of Sciences
    Details
    Publication Date: 2013-07-31
    Description: The monoamine oxidase isoenzymes (MAOs) A and B play important roles in the homeostasis of monoaminergic neurotransmitters. The combined deficiency of MAO A and B results in significantly elevated levels of serotonin (5-hydroxytryptamine), norepinephrine, dopamine, and β-phenylethylamine; in humans and mice, these neurochemical changes are accompanied by neurodevelopmental perturbations as...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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