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  • 1
    Electronic Resource
    Electronic Resource
    Genomic organization and chromosomal localization of the human casein gene family (1997)
    Springer
    Human genetics 〈Berlin〉 99 (1997), S. 368-373 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Five yeast artificial chromosome (YAC) clones containing the human casein gene family were isolated and characterized to study the control mechanisms for the expression of these genes. Partial restriction analysis in conjunction with the chromosomal fragmentation method and fluorescence in situ hybridization (FISH) analysis were performed to construct a detailed physical map of the casein gene family and to determine the chromosomal localization of these genes. The isolated YAC clones 748F3, 750D11, 882G11, 886B3 and 960D2 were 1.2 Mb, 860 kb, 800 kb 1.5 Mb and 1.5 Mb in size, respectively. The clones 748F3, 882G11, 886B3 and 960D2 contained the entire casein gene family, while the κ-casein gene was absent in 750D11. The human αS1-, β- and κ-casein genes were found to be closely linked and arranged in the order αS1-β-κ. The distance between αS1 and β, and between αS1 and κ was approximately 10 and 300 kb, respectively. The β-casein gene was oriented in the opposite direction to the αS1- and κ-casein genes. The casein gene family was localized to chromosome 4q21.1 by FISH analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050374
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  • 2
    Electronic Resource
    Electronic Resource
    Application of a dc glow discharge source with controlled plasma potential in plasma immersion ion implantation (1999)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 86 (1999), S. 4821-4824 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A dc glow discharge source with controlled plasma potential was developed for application in plasma immersion ion implantation processing of materials surfaces. This type of ion implantation system allows cost effective surface modification of workpieces with complex shapes. The effects of the nitrogen plasma etching during the plasma immersion ion implantation process was studied using Si wafers as monitors, as we varied the externally controlled plasma potential between 0 and 350 V. When the plasma potential is controlled below 70 V, the ion implantation is dominant, otherwise the etching overtakes. The nitrogen implanted silicon wafers were analyzed by high resolution x-ray diffraction and Auger electron spectroscopy which revealed successful implantation of ions with accumulated nitrogen dose of 1.5×1017 cm−2, for the low potential case. © 1999 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.371448
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  • 3
    Electronic Resource
    Electronic Resource
    A new concept for coal water mixture stabilization using a polyelectrolyte (1995)
    Springer
    Colloid & polymer science 273 (1995), S. 490-495 
    Details
    ISSN: 1435-1536
    Keywords: Coal water mixture ; sodium polystyrene sulphonate ; depletion stabilization effect ; concentrated dispersion ; dynamic mobility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract The stabilization mechanism of Sodium Polystyrene Sulphonate (PSSNa) on coal water mixture (CWM) has been examined using the following colloid chemical concept. It is realized that the stabilization of the CWM is due to an increase in electrostatic repulsion between the coal particles and the electrostatic repulsion is influenced strongly by the concentration of metal cations, especially Ca2+ eluted from the coal surface. The adsorption isotherm of PSSNa on the coal surface indicates a weak affinity type and the desorption amount of PSSNa is tremendously small in compared with the amount of adsorption. This indicates that a lot of PSSNa adsorbed weakly has been eliminated from the surface in the pre-washing process of desorption experiment. Furthermore, it appears that the ζ-potential determined by the Acoustosizer for concentrated coal suspension shows higher values than the values determined by the usual electrophoresis, and that the high values hold for a wide range of salt concentrations in the medium. All these results indicate that much PSSNa is adsorbed weakly on the coal surface and the component plays a role in the stability character of CWM, where a large contribution of depletion stabilization effect can be expected.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00656894
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  • 4
    Electronic Resource
    Electronic Resource
    A novel heterologous gene expression system in Saccharomyces cerevisiae using the isocitrate lyase gene promoter from Candida tropicalis (1996)
    Springer
    Applied microbiology and biotechnology 44 (1996), S. 759-765 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  We have found that the upstream region of the isocitrate lyase gene (UPR-ICL) from the n-alkane-utilizing yeast Candida tropicalis was functional in Saccharomyces cerevisiae as a novel promoter with non-fermentable carbon sources, such as oleic acid, acetate, ethanol, and glycerol/lactate. The expression of two foreign genes coding for β-galactosidase from Escherichia coli (LacZ) and glutamate decarboxylase from rat brain was carried out under the control of UPR-ICL. Expression of LacZ was repressed by glucose and enhanced over 300-fold by acetate. When an expression vector pWI3 containing multicloning sites between UPR-ICL and the transcriptional terminator of the isocitrate lyase gene (TERM-ICL) was used, the smaller isoform of glutamate decarboxylase (GAD65) was highly produced in a soluble and active form. These results demonstrate that the novel expression system using UPR-ICL and TERM-ICL from C. tropicalis is useful for the production of heterologous proteins in S. cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00178615
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  • 5
    Electronic Resource
    Electronic Resource
    A novel heterologous gene expression system inSaccharomyces cerevisiae using the isocitrate lyase gene promoter fromCandida tropicalis (1996)
    Springer
    Applied microbiology and biotechnology 44 (1996), S. 759-765 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract We have found that the upstream region of the isocitrate lyase gene (UPR-ICL) from then-alkane-utilizing yeastCandida tropicalis was functional inSaccharomyces cerevisiae as a novel promoter with non-fermentable carbon sources, such as oleic acid, acetate, ethanol, and glycerol/lactate. The expression of two foreign genes coding for β-galactosidase fromEscherichia coli (LacZ) and glutamate decarboxylase from rat brain was carried out under the control of UPR-ICL. Expression ofLacZ was repressed by glucose and enhanced over 300-fold by acetate. When an expression vector pW13 containing multicloning sites between UPR-ICL and the transcriptional terminator of the isocitrate lyase gene (TERM-ICL) was used, the smaller isoform of glutamate decarboxylase (GAD65) was highly produced in a soluble and active form. These results demonstrate that the novel expression system using UPR-ICL and TERM-ICL fromC. tropicalis is useful for the production of heterologous proteins inS. cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00178615
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  • 6
    Electronic Resource
    Electronic Resource
    Development of an arming yeast strain for efficient utilization of starch by co-display of sequential amylolytic enzymes on the cell surface (1999)
    Springer
    Applied microbiology and biotechnology 51 (1999), S. 65-70 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The construction of a whole-cell biocatalyst with its sequential reaction has been performed by the genetic immobilization of two amylolytic enzymes on the yeast cell surface. A recombinant strain of Saccharomyces cerevisiae that displays glucoamylase and α-amylase on its cell surface was constructed and its starch-utilizing ability was evaluated. The gene encoding Rhizopus oryzae glucoamylase, with its own secretion signal peptide, and a truncated fragment of the α-amylase gene from Bacillus stearothermophilus with the prepro secretion signal sequence of the yeast α factor, respectively, were fused with the gene encoding the C-terminal half of the yeast α-agglutinin. The constructed fusion genes were introduced into the different loci of chromosomes of S. cerevisiae and expressed under the control of the glyceraldehyde-3-phosphate dehydrogenase promoter. The glucoamylase and α-amylase activities were not detected in the culture medium, but in the cell pellet fraction. The transformant strain co-displaying glucoamylase and α-amylase could grow faster on starch as the sole carbon source than the transformant strain displaying only glucoamylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051364
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  • 7
    Electronic Resource
    Electronic Resource
    Independent production of two molecular forms of a recombinant Rhizopus oryzae lipase by KEX2-engineered strains of Saccharomyces cerevisiae (1999)
    Springer
    Applied microbiology and biotechnology 52 (1999), S. 534-540 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A mixture of rProROL having the full-length prosequence (97 amino acids) for a recombinant lipase of Rhizopus oryzae (rROL) and r28ROL having 28 amino acids of the same prosequence has been produced as active forms by Saccharomyces cerevisiae [Takahashi et al. (1998) J Ferment Bioeng 86: 164–168]. However, the separation of rProROL and r28ROL has not been successful due to their identical behavior on column chromatographs, presumably because of the similarity of their surface properties. The independent production of two different molecular forms of rROL was carried out using KEX2-engineered strains of S. cerevisiae, since r28ROL was predicted to be a product from rProROL by a Kex2-like protease. rProROL was successfully obtained by expression of the ROL gene in the S. cerevisiae kex2 strain in which the KEX2 gene encoding Kex2p was disrupted, while r28ROL was obtained by co-expression of the gene (KEX2Δ613) encoding the soluble form of the C-terminal truncated Kex2 protease (sKex2p). The specific lipase activities of rProROL and r28ROL were 92.9 U/mg and 140 U/mg, respectively. rProROL was stable at pH 2.2–8.0, and showed the optimal reaction temperature to be 30–35 °C with a T 50 of 55 °C (T 50 is the temperature resulting in 50% loss of activity). The values for r28ROL were pH 3.0–10.0, 25–30 °C, and 40 °C, respectively. rProROL was an N-linked glycosylated form, but r28ROL was not. The enhanced thermostability of rProROL did not seem to be due to the N-linked glycosylation, as judged by the results of the Endo H treatment. rProROL had the highest esterase activity toward p-nitrophenyl laurate (C12), whereas r28ROL had the highest esterase activity toward p-nitrophenyl caprylate (C8) and stearate (C18). These results suggest that the distinct properties of these two forms of lipase are caused by the different length of the ROL prosequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051556
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  • 8
    Electronic Resource
    Electronic Resource
    A novel promoter, derived from the isocitrate lyase gene of Candida tropicalis, inducible with acetate in Saccharomyces cerevisiae (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 489-492 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  When the isocitrate lyase gene, containing 5′-upstream and 3′-flanking regions, of an n-alkane-assimilating yeast Candida tropicalis was introduced into Saccharomyces cerevisiae, the enzyme was functionally overexpressed in the cells grown on acetate. The amount of the recombinant isocitrate lyase expressed in S. cerevisiae was as much as 30% of the total soluble proteins in the cells, being comparable to that with GAL7 functional under the control of galactose. The expression was also observed when the cells were grown on glycerol, lactate, ethanol or oleate. These facts indicate that the isocitrate lyase gene upstream region (UPR-ICL) contains a strong promoter functional in S. cerevisiae. UPR-ICL is active as a promoter on cheap carbon sources such as acetate and non-conventional carbon sources such as oleate, whereas many conventional strong promoters demand relatively expensive sugars or sugar derivatives. Therefore, it is promising to construct an economical recombinant protein production system by using UPR-ICL.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050439
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  • 9
    Electronic Resource
    Electronic Resource
    A novel promoter, derived from the isocitrate lyase gene of Candida tropicalis, inducible with acetate in Saccharomyces cerevisiae (1995)
    Springer
    Applied microbiology and biotechnology 43 (1995), S. 489-492 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract When the isocitrate lyase gene, containing 5'-upstream and 3'-flanking regions, of an n-alkane-assimilating yeast Candida tropicalis was introduced into Saccharomyces cerevisiae, the enzyme was functionally overexpressed in the cells grown on acetate. The amount of the recombinant isocitrate lyase expressed in S. cerevisiae was as much as 30% of the total soluble proteins in the cells, being comparable to that with GAL7 functional under the control of galactose. The expression was also observed when the cells were grown on glycerol, lactate, ethanol or oleate. These facts indicate that the isocitrate lyase gene upstream region (UPR-ICL) contains a strong promoter functional in S. cerevisiae. UPR-ICL is active as a promoter on cheap carbon sources such as acetate and nonconventional carbon sources such as oleate, whereas many conventional strong promoters demand relatively expensive sugars or sugars derivatives. Therefore, it is promising to construct an economical recombinant protein production system by using UPL-ICL.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218454
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  • 10
    Electronic Resource
    Electronic Resource
    Genetic immobilization of cellulase on the cell surface of Saccharomyces cerevisiae (1997)
    Springer
    Applied microbiology and biotechnology 48 (1997), S. 499-503 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract We tried genetically to immobilize cellulase protein on the cell surface of the yeast Saccharomyces cerevisiae in its active form. A cDNA encoding FI-carboxymethylcellulase (CMCase) of the fungus Aspergillus aculeatus, with its secretion signal peptide, was fused with the gene encoding the C-terminal half (320 amino acid residues from the C terminus) of yeast α-agglutinin, a protein involved in mating and covalently anchored to the cell wall. The plasmid constructed containing this fusion gene was introduced into S. cerevisiae and expressed under the control of the glyceraldehyde-3-phosphate dehydrogenase promoter from S. cerevisiae. The CMCase activity was detected in the cell pellet fraction. The CMCase protein was solubilized from the cell wall fraction by glucanase treatment but not by sodium dodecyl sulphate treatment, indicating the covalent binding of the fusion protein to the cell wall. The appearance of the fused protein on the cell surface was further confirmed by immunofluorescence microscopy and immunoelectron microscopy. These results proved that the CMCase was anchored on the cell wall in its active form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051086
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