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  • 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
    Existence of an α-chymotrypsin-like immunoreactivity in bovine mast cells (1982)
    Springer
    Cellular and molecular life sciences 38 (1982), S. 277-278 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Using an indirect fluorescent antibody technique, we detected an α-chymotrypsin-like immunoreactivity, but no trypsin-like immunoreactivity in bovine mast cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01945111
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  • 5
    Electronic Resource
    Electronic Resource
    A new, rapid and precise method for measuring the intra-cellular water content by gas chromatography and3H-sucrose (1981)
    Springer
    Cellular and molecular life sciences 37 (1981), S. 748-750 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A new rapid method for measuring intra-cellular water content by gas chromatography and an isotopic (3H-sucrose) technique is described. Water content of circulating red cells was revealed to be 71.26±0.31%. Intra-cellular water content increased to 102.9% of its original value following addition of 3 volumes of acid-citrate-dextrose (ACD) to 20 volumes of blood.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01967959
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  • 6
    Electronic Resource
    Electronic Resource
    Inhibition ofα-chymotrypsin by 2-halogeno-ethanols; comparison with 2-methyl-ethanols and urea (1979)
    Springer
    Cellular and molecular life sciences 35 (1979), S. 1011-1012 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 2-Halogeno- and 2-methyl-ethanols inhibitα-chymotrypsin in the order of their substituted groups: [1] tri〉di-〉mono-, [2] Br-〉Cl-〉CH3-〉F-. The inhibition by the halogeno-ethanols is mediated differently from that by the methyl-ethanols, ethanol, and urea.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01949911
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  • 7
    Electronic Resource
    Electronic Resource
    A new runaway type episomal vector for mammalian cells based on a temperature-sensitive simian virus 40 and inducible erythropoietin production (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 591-596 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A runaway vector for mammalian cells was constructed from the simian virus 40 (SV40) genome with a temperature-sensitive mutation of the large T antigen and bacterial neo r gene. Replication of this plasmid was repressed above 39°C and vigorous DNA propagation was observed below 33°C in simian CV-1 cells. The human erythropoietin gene was inserted downstream of the SV40 late promoter of the plasmid and the recombinant plasmid was introduced into CV-1 cells. By a temperature shift from 37 to 33°C, the plasmid copy number increased from 5 × 102 to 5 × 103 copies per cell and the specific production rate of erythropoietin increased more than ten-fold. The bacterial-derived sequences such as the neo r gene and vector pUC sequences were prone to delete but the main body of the recombinant plasmid such as SV40 and the erythropoietin-coding sequences were stably maintained at either 33 or 37°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00178495
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  • 8
    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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  • 9
    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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  • 10
    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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