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  • 1
    Electronic Resource
    Electronic Resource
    Centrifugal mass separation in rotating plasmas produced by a coaxial plasma gun (1989)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 55 (1989), S. 1289-1291 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: Rotating Cu/Zn plasmas produced by a coaxial plasma gun have been applied to plasma centrifuge. A separation factor of up to 10 is measured over a radius of 4 cm when a current of 13 kA and an axial magnetic field of 2.5 kG are applied. Plasma parameters are: rotation frequency ω=1.1×106 rad/s, density n∼1015 cm−3, and ion temperature Ti=10 eV. The separation factor of 2 is attained even in the plasma core where the density is higher than one-half of the peak value. This is attributed to the fact that a strong centrifugal force forms a hollow density profile which gives the density peak at a radius of 2 cm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.101635
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  • 2
    Electronic Resource
    Electronic Resource
    On the mechanism of dimensional change of neutron irradiated graphite (1992)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 61 (1992), S. 1638-1640 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: In order to investigate the mechanism of large volume expansion of graphite due to neutron irradiation we have made in situ observation of damage structure of graphite with a high resolution transmission electron microscope (HRTEM). Both bending and randomizing the orientation of broken basal planes are proposed to be the origin for the large volume expansion of the irradiated graphite. It is also found that graphite easily loses its lattice ordering in the basal planes as demonstrated by halo rings in the (101¯0) diffraction pattern, while hardly losing its layered structure, i.e., (002) spots are retained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.108436
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  • 3
    Electronic Resource
    Electronic Resource
    Grain formation experiments by a plasma jet apparatus (1986)
    Springer
    Astrophysics and space science 119 (1986), S. 147-149 
    Details
    ISSN: 1572-946X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00648834
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  • 4
    Electronic Resource
    Electronic Resource
    A quenched carbonaceous composite (QCC) grain model for the interstellar 220 NM extinction hump (1986)
    Springer
    Astrophysics and space science 118 (1986), S. 411-413 
    Details
    ISSN: 1572-946X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The dependence of the wavelength of peak absorption of dust grains on the grain size is investigated analytically by using an oscillator model for the absorption band. The peak wavelength of a weak absorption band is much less sensitive to the grain size than that of a strong band. This is explained by the fact that the surface mode, which is excited in the strong absorption band, is not raised in the weak absorption band. A quenched carbonaceous composite (QCC) synthesized from hydrocarbon plasma is found to have a weak absorption band at 220 nm. The absorption peak wavelength of the QCC grains falls well in the range of 217±7 nm even if the grain size runs from 5 to 100 nm. This is compatible with the observed constancy of the 220 nm hump (217±5 nm). By contrast, the absorption peak of graphite grains, which have a strong band around 280 nm and have been investigated as candidates for the hump, is very sensitive to the grain size. A quite narrow range of the grain size is required to account for the observed 220 nm feature. A weak absorption model, such as the QCC grains, is suggested to be a more likely candidate for the 220 nm extinction hump than a strong absorption model, such as graphite grains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00651159
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  • 5
    Electronic Resource
    Electronic Resource
    Action of metalloproteinases on porcine dentin mineralization (1994)
    Springer
    Calcified tissue international 55 (1994), S. 426-435 
    Details
    ISSN: 1432-0827
    Keywords: Dentin mineralization ; Enzymography ; Geatinases ; Proteoglycanases ; Protoglycans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Samples containing predentin and mineralized dentin involving the mineralized front (newly formed dentin) were prepared by scraping developing porcine teeth after odontoblastic cell debris had been removed from the predentin surfaces. An extract was obtained separately from the matrices of predentin and of the newly formed dentin with a 4 M guanidine solution before and after demineralization with acetic acid solution. Enzymography detected 56 and 61 kDa gelatinases and 25 kDa proteoglycanase as neutral metalloproteinases in both extracts and proved them to be in an active form. Approximately half of the 56 and 61 kDa gelaunases binds to collagen fibers in predentin matrix. Three high molecular weight proteoglycans (70–85 kDa, 130–180 kDa, and 290 kDa) were found in the predentin matrix, but not in the newly formed dentin. The proteoglycanases in predentin degraded 290 kDa proteoglycan, if incubated together with calcium (Ca) ions. The results of this investigation indicate that active proteoglycanases with existed in the predentin perform no substantial work in proteoglycan degradation because the Ca ions are masked in the predentin matrix by coexisting proteoglycans. When mineralization occurs, however, they can degrade the proteoglycan at the mineralization front because excess Ca ions may be supplied via odontoblastic processes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00298556
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  • 6
    Electronic Resource
    Electronic Resource
    The localization and characterization of proteinases for the initial cleavage of porcine amelogenin (1992)
    Springer
    Calcified tissue international 51 (1992), S. 213-217 
    Details
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Degradation of amelogenin ; Proteinases ; 25kDa amelogenin ; Enzymography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary In the outermost layer of porcine-developing enamel adjacent to the ameloblasts in the secretory stage, the activities of two proteinases having molecular masses of 76 and 78kDa were detected by enzymography using gelatin as a substrate. On the other hand, high activities of known 30 and 34kDa proteinases were localized in the inner layer of the enamel. The 76kDa proteinase cleaved the carboxylterminal peptide of porcine 25kDa amelogenin to convert it to 20kDa amelogenin. The 78kDa proteinase also acted on the 25kDa amelogenin similarly, but its activity was weak. The results indicate that the 25kDa amelogenin synthesized and secreted by ameloblasts is converted to 20kDa amelogenin by the action of proteinase localized in the outermost layer of the secretory enamel, and then further degraded by the proteinases in the inner layer of the enamel associated with the increase of mineralization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334549
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  • 7
    Electronic Resource
    Electronic Resource
    Enamelins in the newly formed bovine enamel (1993)
    Springer
    Calcified tissue international 53 (1993), S. 257-261 
    Details
    ISSN: 1432-0827
    Keywords: Bovine enamelin ; Amelogenin ; Newly formed enamel ; Western blot
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The possibility of using the antisera raised in rabbits against the porcine 25 kDa amelogenin, 32 and 89 kDa enamelins, and the 13–17 kDa nonamelogenin for the differentiation and identification of the protein components in bovine immature enamel was examined. Although the immunoreactivities of these antisera against bovine enamel proteins were weaker than those against the porcine proteins, it was found that these antisera could differentiate and demonstrate immunohistochemically a characteristic distribution of three different kinds of enamel protein components in the bovine secretory stage enamel similar to those observed in the porcine immature enamel. Of the several high molecular weight proteins being reactive to the anti-porcine 32 and 89 kDa enamelin sera, the 130 kDa protein, having the highest molecular weight, was extracted and purified from the bovine enamel sample which was obtained by peeling approximately 30-μm thickness of the outermost layer of the secretory stage enamel. The amino acid composition of the 130 kDa protein was similar to the known bovine enamelins, and was rich in aspartic acid, glutamic acid, proline, and glycine. The results could suggest that the enamelins of lower molecular weight than this protein, which are found in the bovine secretory stage enamel, are derived from this precursor protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01320911
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  • 8
    Electronic Resource
    Electronic Resource
    Porcine amelogenins (1994)
    Springer
    Calcified tissue international 54 (1994), S. 69-75 
    Details
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine amelogenin ; Plasma desorption mass spectometry ; Amino acid sequence ; CNBr cleavage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316293
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  • 9
    Electronic Resource
    Electronic Resource
    Combined method of fluorescence tracer technique and PAP immunohistochemistry for discrimination of the transplanted cells (1989)
    Springer
    Histochemistry and cell biology 91 (1989), S. 191-194 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The retrograde fluorescence tracer, True Blue (TB), was injected into the forebrain septal area of neonatal rats. After 3 to 6 days the brains of these animals were carefully removed and placed in ice-cold sterilized physiological saline containing 1% glucose. Under the surgical microscope, one or two pairs of mesencephalic tissue samples, each containing a dorsal raphe nucleus, were punched out and transplanted into the third ventricle of a 5,6-DHT-pretreated adult rat. One month after transplantation, all animals were perfused and their brains sectioned using a cryostat. The sections were examined using a fluorescence microscope, and then processed for serotonin immunohistochemistry. The grafts were found to be successfully implanted and connected with the middle portion of the third ventricle. Four types of neurons, i.e., TB-labeled, serotonin-labeled, both TB-and serotonin-labeled, and non-labeled neurons, were detected in the grafts. This double-labeling method is considered to be a useful technique in characterizing the neurons in grafts which consist of a heterogeneous cell population.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490131
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  • 10
    Electronic Resource
    Electronic Resource
    Immunochemical and immunohistochemical studies, using antisera against porcine 25 kDa amelogenin, 89 kDa enamelin and the 13–17 kDa nonamelogenins, on immature enamel of the pig and rat (1991)
    Springer
    Histochemistry and cell biology 96 (1991), S. 129-138 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Enamel proteins were extracted from the newly formed layer of immature porcine enamel, and the 25 kDa amelogenin, 89 kDa enamelin and 13–17 kDa nonamelogenins were purified. Specific antisera were raised against these proteins. Antibodies specific to the C-terminal region (residues 149–173) of the 25 kDa amelogenin were generated by absorption of the anti-25 kDa amelogenin serum with 20 kDa amelogenin, which contains residues 1–148 of the antigen. Immunoelectrotransfer blotting of the extracted porcine enamel proteins showed that the anti-25 kDa amelogenin serum recognized the 25 kDa and other low and high molecular weight amelogenins. The C-terminal specific anti-25 kDa amelogenin serum reacted only with amelogenins having molecular weights over 23 kDa. The anti-89 kDa enamelin serum recognized the 89 kDa enamelin and lower molecular weight proteins, but neither the amelogenins nor the 13–17 kDa nonamelogenins. The antiserum against the 13–17 kDa nonamelogenins showed no cross reactivity to the 89 kDa enamelin, but recognized higher molecular weight nonamelogenins. In immunohistochemical preparations of the porcine tooth germs, the 25 kDa amelogenin-like immunoreactivity over immature enamel decreased in a gradient from the enamel surface to the middle layer. In the inner layer immunoreactivity was concentrated over the prism sheaths. The C-terminal specific 25 kDa amelogenin-like immunoreactivity was intense at the outer layer of immature enamel and decreased sharply toward the middle layer. Prism sheaths were intensely stained by the antiserum to the 13–17 kDa nonamelogenins. The 89 kDa enamelin-like immunoreactivity over enamel prisms was intense at the outer layer and decreased toward the middle layer. Staining by the anti-89 kDa enamelin serum of prism sheaths was faint. In immature rat incisor enamel, the C-terminal specific 25 kDa amelogenin antiserum demonstrated a staining pattern similar to that in the immature enamel of the pig. Distinct 13–17 kDa nonamelogenin-like and 89 kDa enamelin-like immunoreactivities were found especially in the layer adjacent to the Tomes' process. We conclude that some enamel proteins are degraded soon after their secretion from the secretory ameloblast in the rat and the pig. The specific enamel proteins which reacted with the antiserum to the 13–17 kDa nonamelogenins seem to be involved with the formation of prism sheaths in immature porcine enamel, but not in rat incisor enamel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00315983
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