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  • Springer  (116)
  • Springer Nature  (2)
  • American Meteorological Society  (1)
  • 1995-1999  (119)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Inhibitory conditioning for carrot somatic embryogenesis in high-cell-density cultures (1998)
    Springer
    Plant cell reports 18 (1998), S. 2-6 
    Details
    ISSN: 1432-203X
    Keywords: Key words Carrot ; Somatic embryogenesis ; Conditioned medium ; High-cell-density culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Carrot somatic embryogenesis was strongly inhibited in high-cell-density cultures. This inhibition was not caused by depletion of nutrients or physical damage but by factor(s) released into the culture medium from cells during culture. A conditioned medium prepared by eliminating cells after high-cell-density culture inhibited somatic embryogenesis. The degree of inhibition increased with the amount of conditioned medium. A dialysis experiment revealed that the molecular weight of the inhibiting factor(s) was below 3,500. We also found that the conditioned medium contained a high-molecular-weight factor(s), which stimulated somatic embryogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050522
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  • 2
    Electronic Resource
    Electronic Resource
    Genetic relationships of pilchards (genus: Sardinops) with anti-tropical distributions (1996)
    Springer
    Marine biology 126 (1996), S. 585-590 
    Details
    ISSN: 1432-1793
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The pilchards (genus Sardinops), one of the major components of the world's harvest of fishes, is distributed sporadically in the temperate zone on a global scale. Mitochondrial DNA variation in 95 pilchards from nine worldwide localities in five current systems was examined using ten restriction enzymes. Although several opinions have been proposed on the global population structure of the genus Sardinops, our results clearly rejected the hypothesis of gene flow among geographically distant populations on a global scale. Results indicate that the Japanese pilchards and the Australian and South African pilchards were derived from the eastern Pacific populations, following the speciation of Sardinops in the Pacific, after the formation of the Isthmus of Panama. An intermixing of the northeastern and southeastern Pacific populations during the Pleistocene glacial maxima is suggested from their genetic affinities.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351325
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  • 3
    Electronic Resource
    Electronic Resource
    A vanishing theorem for modular symbols on locally symmetric spaces (1998)
    Springer
    Commentarii mathematici Helvetici 73 (1998), S. 45-70 
    Details
    ISSN: 1420-8946
    Keywords: Key words. Modular symbols, semisimple Lie group, Zuckerman-Vogan module, Matsushima-Murakami formula, modular varieties, discrete decomposable restriction, bounded symmetric domain, discontinuous group, symmetric space.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract. A modular symbol is the fundamental class of a totally geodesic submanifold $ \Gamma'\backslash G'/K' $ embedded in a locally Riemannian symmetric space $ \Gamma \backslash G / K $ , which is defined by a subsymmetric space $ G'/ K' \hookrightarrow G / K $ . In this paper, we consider the modular symbol defined by a semisimple symmetric pair (G,G'), and prove a vanishing theorem with respect to the $ \pi $ -component $ (\pi \in \widehat {G}) $ in the Matsushima-Murakami formula based on the discretely decomposable theorem of the restriction $ \pi |_{G'} $ . In particular, we determine explicitly the middle Hodge components of certain totally real modular symbols on the locally Hermitian symmetric spaces of type IV.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000140050045
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16 (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 473-481 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala-Gln-Ser-Val-Pro-Trp-Gly-Ile-Ser-Arg-Val-Gln-Ala-Pro-Ala-Ala-His-Asn-Arg-Gly-Leu-Thr-Gly. The molecular mass of the protease was 28 kDa, and its isoelectric point was close to pH 10.6. Maximum activity toward casein was observed at 55°C and at pH 12.3 in 50 mM phosphate/NaOH buffer. The activity was inhibited by phenylmethylsulfonyl flouride and chymostatin. The enzyme was very stable in long-term incubation with liquid detergents at 40°C. The enzyme cleaved the oxidized insulin B chain initially at Leu15-Tyr16 and efficiently at ten more sites. Among various oligopeptidyl p-nitro-anilides (pNA) tested, N-succinyl-Ala-Ala-Pro-Phe-pNA was efficiently hydrolyzed by M protease. M protease was precipitated in (NH4)2SO4-saturated acetate buffer (pH 5.0) as plank-like cyrstals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218452
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  • 5
    Electronic Resource
    Electronic Resource
    Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16 (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 473-481 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Alkaline protease (EC 3.4.21.14) activity, suitable for use in detergents, was detected in the alkaline culture medium of Bacillus sp. KSM-K16, which was originally isolated from soil. The enzyme, designated M protease, was purified to homogeneity from the culture broth by column chromatographies. The N-terminal amino acid sequence was Ala–Gln–Ser–Val–Pro–Trp–Gly–Ile–Ser–Arg–Val–Gln–Ala–Pro–Ala–Ala–His–Asn–Arg–Gly–Leu–Thr–Gly. The molecular mass of the protease was 28 kDa, and its isoelectric point was close to pH 10.6. Maximum activity toward casein was observed at 55 °C and at pH 12.3 in 50 mM phosphate/NaOH buffer. The activity was inhibited by phenylmethylsulfonyl fluoride and chymostatin. The enzyme was very stable in long-term incubation with liquid detergents at 40 °C. The enzyme cleaved the oxidized insulin B chain initially at Leu15–Tyr16 and efficiently at ten more sites. Among various oligopeptidyl p-nitro-anilides (pNA) tested, N-succinyl-Ala-Ala-Pro-Phe-pNA was efficiently hydrolyzed by M protease. M protease was precipitated in (NH4)2SO4-saturated acetate buffer (pH 5.0) as plank-like crystals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050437
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  • 6
    Electronic Resource
    Electronic Resource
    Purification of alkaline proteases from a Bacillus strain and their possible interrelationship (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 63-71 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  Alkalophilic Bacillus sp. KSM-K16 produced three alkaline proteases, as detected by polyacrylamide gel electrophoresis (PAGE). The major protease, designated M protease, was recently purified to homogeneity and its properties were characterized. In the present study, two minor proteases, designated H protease and N protease, were purified to homogeneity from cultures of this organism. H protease had a molecular mass of 28 kDa, as estimated by sodium dodecyl sulfate/PAGE (SDS-PAGE) and its maximum activity against casein was observed at pH 11.0 and at 55°C. N protease consisted of two polypeptide chains with molecular masses of 12.5 kDa and 14.5 kDa, as estimated by SDS-PAGE, although it migrated as a single protein band during non-denaturing PAGE. Its maximum activity was observed at pH 11.0 and at 60°C. The amino-terminal sequences of H protease and of the 14.5-kDa polypeptide of N protease were identical to that of M protease. The electrophoretic relationship between the three enzymes was examined after they had been stored at different pH values and at 5°C. M protease was converted to H protease more rapidly at pH 11 than at pH 8 or below, and H protease was converted to M protease at pH 8 or below but not at pH 11. N protease appeared to be the autolytic product of the M and H proteases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050650
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  • 7
    Electronic Resource
    Electronic Resource
    Formaldehyde Levels in Rain Water from Kobe City in Japan (1996)
    Springer
    Bulletin of environmental contamination and toxicology 57 (1996), S. 556 -559 
    Details
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001289900226
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  • 8
    Electronic Resource
    Electronic Resource
    Vanadium Content of Cigarettes (1998)
    Springer
    Bulletin of environmental contamination and toxicology 61 (1998), S. 276-280 
    Details
    ISSN: 1432-0800
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001289900759
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  • 9
    Electronic Resource
    Electronic Resource
    High levels of non-methylesterified pectins and low levels of peripherally located pectins in loosely attached non-embryogenic callus of carrot (1999)
    Springer
    Plant cell reports 18 (1999), S. 561-566 
    Details
    ISSN: 1432-203X
    Keywords: Key words Callus ; Cell wall ; Daucus carota ; Intercellular attachment ; Pectin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Carrot embryogenic callus (EC) forms larger and tighter clusters of cells than does non-embryogenic callus (NC). Morphological and histochemical analyses of EC and NC were made using the electron microscope. The entire cell wall in NC was strongly stained by ruthenium red, which reacts primarily with carboxyl groups of acidic sugars. By contrast, in EC, strong staining by ruthenium red of the entire cell wall, of amorphous structures on the surface of EC and of secretory vesicles was observed only after treatment with NaOH. Scanning electron microscopy revealed the presence of amorphous structures on the entire surface of EC but not of NC. These results suggest the abundance of non-methylesterified pectins and the presence of methylesterified and peripherally located pectins in the cell walls of NC and EC, respectively, as well as the absence, in carrot cultured cells, of any correlation between the calcium bridges of pectins and intercellular attachment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050622
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  • 10
    Electronic Resource
    Electronic Resource
    Observation of a proton halo in8B (1995)
    Springer
    The European physical journal 350 (1995), S. 283-284 
    Details
    ISSN: 1434-601X
    Keywords: 27.20+n ; 21.10.Ft ; 29.30−h ; 21.60−n
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The longitudinal momentum distribution of7Be was measured after the break-up reaction of8B in C, Al, and Pb targets at 1471 A·MeV. We observed a narrow distribution with a FWHM of (81±6) MeV/c in all targets. The experimental results indicate an extended spatial distribution of the loosely bound proton in8B, and agree with QRPA calculations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01291183
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