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  • 2000-2004  (2)
  • 1990-1994  (6)
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  • 1
    Digitale Medien
    Digitale Medien
    Presence of carnitine acetyltransferase in peroxisomes and in mitochondria of oleic acid-grown Saccharomyces cerevisiae (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 112 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Abstract Activity of carnitine acetyltransferase was detected in glucose- and oleic acid-grown Saccharomyces cerevisiae. Oleic acid-grown cells showed a ten-fold higher activity than glucose-grown cells. Subcellular fractionation of oleic acid-grown cells showed that carnitine acetyltransferase was present in peroxisomes, mitochondria, and cytosol. The results suggested the plausible presence of an ‘acetylcarnitine shuttle’ in this yeast, as in the case of an n-alkane-assimilating yeast, Candida tropicalis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06419.x
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  • 2
    Digitale Medien
    Digitale Medien
    Effect of catalase-specific inhibitor 3-amino-1,2,4-triazole on yeast peroxisomal catalase in vivo (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 219 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: 3-Amino-1,2,4-triazole (3-AT) is known as an inhibitor of catalase to whose active center it specifically and covalently binds. Subcellular fractionation and immunoelectronmicroscopic observation of the yeast Candida tropicalis revealed that, in 3-AT-treated cells in which the 3-AT was added to the n-alkane medium from the beginning of cultivation, catalase transported into peroxisomes was inactivated and was present as insoluble aggregated forms in the organelle. The aggregation of catalase in peroxisomes occurred only in these 3-AT-treated cells and not in cells in which 3-AT was added at the late exponential growth phase. Furthermore, 3-AT did not affect the transportation of catalase into peroxisomes. The appearance of aggregation only in cells to which 3-AT was added from the beginning of cultivation suggests that, in the process of catalase transportation into yeast peroxisomes, some conformational change may take place and that correct folding may be inhibited by the binding of 3-AT to the active center of catalase. Accordingly, 3-AT will be an interesting compound for investigation of the transport machinery of the peroxisomal tetrameric catalase.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1016/S0378-1097(02)01201-6
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  • 3
    Digitale Medien
    Digitale Medien
    Cytochemical evaluation of localization and secretion of a heterologous enzyme displayed on yeast cell surface (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 192 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: A starch-utilizing Saccharomyces cerevisiae strain was constructed by cell surface engineering. Distribution of the heterologous glucoamylase–α-agglutinin fusion protein on the yeast cell was analyzed by indirect fluorescence microscopy using an anti-glucoamylase antibody. Most of the intense fluorescence was first localized in the small bud, then observed on the entire cell wall of the daughter and mother cells. Fluorescence also accumulated at the neck region. These observations suggest that the display of the heterologous protein on the cell surface is carried with other cell wall components to the areas in which the cell wall is newly synthesized; the distribution is controlled by the cell cycle. Then, the heterologous protein-encoding gene was expressed in a sec1 mutant, in which secretory vesicles accumulate under restrictive temperature, and the produced protein was detected by immunoelectron microscopy. Most of the gold particles that reacted with the fusion protein were not localized in vesicles but in expanding endoplasmic reticulum. This phenomenon may be due to overproduction of the heterologous protein which was designed to be displayed on the cell wall. Artificial production of heterologous protein may have caused a relative shortage of glycosyl phosphatidylinositol anchors.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb09389.x
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  • 4
    Digitale Medien
    Digitale Medien
    Characterization of the catalase of the n-alkane-utilizing yeast Candida tropicalis functionally expressed in Saccharomyces cerevisiae (1994)
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 682-686 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract. Candida tropicalis catalase (CTC) genomic DNA was recombined on a plasmid with the galactose-inducible GAL7 promoter and expressed highly as a heme protein in Saccharomyces cerevisiae as host. The percentage of recombinant CTC (rCTC) in total extractable protein amounted to at least 25%. The rCTC was purified and characterized in terms of subunit mass, behavior in native polyacrylamide gel electrophoresis, absorption spectrum, amino-terminal amino acid sequence, peptide map, specific activity, and Michaelis constant (K m) value for hydrogen peroxide. These properties were similar or identical to those of the purified enzyme from C. tropicalis (CTC). From these results, this system appears suitable for high expression of functional catalase protein having heme.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002530050050
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  • 5
    Digitale Medien
    Digitale Medien
    Peptide synthesis with halophenylalanines by thermolysin (1994)
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 653-656 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract. Thermolysin was able to catalyze enantioselective peptide synthesis with non-natural amino acids, halophenylalanines. However, the reactivity of thermolysin was considerably influenced by the kind and position of halogen substituents on these analogues. The manner of the recognition of the amino component by the enzyme was different from that of the carboxyl component in the synthesis of peptides with non-natural phenylalanine analogues. The phenomena observed are discussed, based on the kinetic parameters obtained.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002530050045
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 6
    Digitale Medien
    Digitale Medien
    Peptide synthesis with halophenylalanines by thermolysin (1994)
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 653-656 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract Thermolysin was able to catalyze enantioselective peptide synthesis with non-natural amino acids, halophenylalanines. However, the reactivity of thermolysin was considerably influenced by the kind and position of halogen substituents on these analogues. The manner of the recognition of the amino component by the enzyme was different from that of the carboxyl component in the synthesis of peptides with non-natural phenylalanine analogues. The phenomena observed are discussed, based on the kinetic parameters obtained.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00173324
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  • 7
    Digitale Medien
    Digitale Medien
    Characterization of the catalase of the n-alkane-utilizing yeast Candida tropicalis functionally expressed in Saccharomyces cerevisiae (1994)
    Springer
    Applied microbiology and biotechnology 40 (1994), S. 682-686 
    Details
    ISSN: 1432-0614
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Werkstoffwissenschaften, Fertigungsverfahren, Fertigung
    Notizen: Abstract Candida tropicalis catalase (CTC) genomic DNA was recombined on a plasmid with the galactose-inducible GAL7 promoter and expressed highly as a heme protein in Saccharomyces cerevisiae as host. The percentage of recombinant CTC (rCTC) in total extractable protein amounted to at least 25%. The rCTC was purified and characterized in terms of subunit mass, behavior in native polyacrylamide gel electrophoresis, absorption spectrum, amino-terminal amino acid sequence, peptide map, specific activity, and Michaelis constant (K m) value for hydrogen peroxide. These properties were similar or identical to those of the purified enzyme from C. tropicalis (CTC). From these results, this system appears suitable for high expression of functional catalase protein having heme.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00173329
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 8
    Digitale Medien
    Digitale Medien
    High level expression of isocitrate lyase gene of n-alkane-utilizing yeast Candida tropicalis in Sacchromyces cerevisiae (1991)
    Springer
    Archives of microbiology 156 (1991), S. 439-443 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Candida tropicalis ; Saccharomyces cerevisiae ; Peroxisomes ; Isocitrate lyase ; GAL7 promoter ; High level expression
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The genomic DNA of peroxisomal isocitrate lyase (ICL) isolated from an n-alkane-assimilating yeast, Candida tropicalis, was truncated to utilize the original open reading frame under the control of the GAL7 promoter and was expressed in Saccharomyces cerevisiae. The recombinant ICL was synthesized as a functionally active enzyme with a specific activity similar to the enzyme purified from C. tropicalis, and was accounted for approximately 30% of the total extractable proteins in the yeast cells. This recombinant enzyme was easily purified to homogeneity. N-Terminal amino acid sequence, molecular masses of native form and subunit, amino acid composition, peptide maps, and kinetic parameters of the recombinant ICL were essentially the same as those of ICL purified from C. tropicalis. From these facts, S. cerevisiae was suggested to be an excellent microorganism to highly express the genes encoding peroxisomal proteins of C. tropicalis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00245389
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