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  • 1
    Monograph available for loan
    Monograph available for loan
    Environmental policy : soil protection policies within the european union (1999)
    Bonn : Selbstverlag
    Details Availability
    Call number: PIK N 071-99-0141
    Type of Medium: Monograph available for loan
    Pages: 507 S.
    Location: A 18 - must be ordered
    Branch Library: PIK Library
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  • 2
    Electronic Resource
    Electronic Resource
    Transport Mutants and Transport Genes of Corynebacterium glutamicum (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 782 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb40560.x
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  • 3
    Electronic Resource
    Electronic Resource
    Construction of l-Lysine-, l-Threonine-, or l-Isoleucine-Overproducing Strains of Corynebacterium glutamicum (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 782 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb40544.x
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  • 4
    Electronic Resource
    Electronic Resource
    Adaptation of the filamentous fungus Ashbya gossypii to hyperosmotic stress: different osmoresponse to NaCl and mannitol stress (1998)
    Springer
    Applied microbiology and biotechnology 50 (1998), S. 219-226 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Osmoadaption mechanisms of the biotechnologically important hemiascomycete Ashbya gossypii were investigated, thereby distinguishing between halo- and osmotolerance by exposure to NaCl and mannitol stress. We studied the growth and ultrastructure of differently treated cells and quantified the intracellular contents of compatible solutes and inorganic ions. Mannitol affected growth of A. gossypii at concentrations above 0.8 M, whereas NaCl inhibited growth at 0.2 M. NaCl-treated cells differed from control cells in having smaller vacuoles, which occupied a smaller part of the cell volume. Glycerol was found to be the predominant compatible solute in A. gossypii; accumulation of inorganic ions could not be detected. Measurement of glycerol uptake under isosmotic conditions as well as upon hyperosmotic stress revealed the existence of a highly active glycerol-uptake system, which, however, was down-regulated under hyperosmotic stress. Investigation of glycerol biosynthesis by measuring glycerol-3-phosphate dehydrogenase activity under hyperosmotic conditions indicated that accumulation of glycerol in A. gossypii is almost solely due to biosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051280
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  • 5
    Electronic Resource
    Electronic Resource
    DNA hydrolysis by inorganic catalysts (1999)
    Springer
    Applied microbiology and biotechnology 52 (1999), S. 761-767 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Non-enzymatic reagents that efficiently promote the hydrolytic cleavage of DNA currently receive much attention since they have many potential applications in molecular biology. This review focuses on recent progress in the hydrolysis of the phosphodiester backbone of DNA by metal ions and metal complexes. Pioneering work on the sequence-selective DNA scission by an artificial restriction enzyme, which is prepared by covalent attachment of a cerium(IV) complex to an antisense-deoxyoligonucleotide, is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051588
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  • 6
    Electronic Resource
    Electronic Resource
    Glutamine uptake by a sodium-dependent secondary transport system in Corynebacterium glutamicum (1995)
    Springer
    Archives of microbiology 164 (1995), S. 98-103 
    Details
    ISSN: 1432-072X
    Keywords: Key words Glutamine ; Amino acid transport ; Solute ; uptake ; Corynebacterium glutamicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Corynebacterium glutamicum took up glutamine by a sodium-dependent secondary transport system. Both the membrane potential and the sodium gradient were driving forces. Glutamine uptake showed Michaelis-Menten kinetics, with a K m of 36 μM and a V max of 12.5 nmol min–1 (mg dry weight)–1 at pH 7. Despite a pH optimum in the alkaline range around pH 9, it was shown that uncharged glutamine is the transported species. The affinity for the cotransported sodium was relatively low; an apparent K m of 1.4 mM was determined. Among various substrates tested, only asparagine, when added in 50-fold excess, led to an inhibition of glutamine transport. It was concluded that glutamine uptake occurs via a specific transport system in symport with at least one sodium ion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050240
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  • 7
    Electronic Resource
    Electronic Resource
    Threonine diffusion and threonine transport in Corynebacterium glutamicum and their role in threonine production (1996)
    Springer
    Archives of microbiology 165 (1996), S. 48-54 
    Details
    ISSN: 1432-072X
    Keywords: Key words Amino acid transport ; Uptake ; Excretion ; Diffusion ; Threonine ; Corynebacterium glutamicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Transmembrane threonine fluxes (i.e., uptake, diffusion, and carrier-mediated excretion) all contribut-ing to threonine production by a recombinant strain of Corynebacterium glutamicum, were analyzed and quantitated. A threonine-uptake carrier that transports threonine in symport with sodium ions was identified. Under production conditions (i.e., when internal threonine is high), this uptake system catalyzed predominantly threonine/threonine exchange. Threonine export via the uptake system was excluded. Threonine efflux from the cells was shown to comprise both carrier-mediated excretion and passive diffusion. The latter process was analyzed after inhibition of all carrier-mediated fluxes. Threonine diffusion was found to proceed with a first-order rate constant of 0.003 min–1 or 0.004 μl min–1 (mg dry wt.)–1, which corresponds to a permeability of 8 × 10–10 cm s–1. According to this permeability, less than 10% of the efflux observed under optimal conditions takes place via diffusion, and more than 90% must result from the activity of the excretion carrier. In addition, the excretion carrier was identified by (1) inhibition of its activity by amino acid modifying reagents and (2) its dependence on metabolic energy in the form of the membrane potential. Activity of the excretion system depended on the membrane potential, but not on the presence of sodium ions. Threonine export in antiport against protons is proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050295
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation of the putP gene of Corynebacterium glutamicum and characterization of a low-affinity uptake system for compatible solutes (1997)
    Springer
    Archives of microbiology 168 (1997), S. 143-151 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsCorynebacterium glutamicum ; PutP ; Proline transport ; Compatible solutes ; Osmoregulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Corynebacterium glutamicum accumulates the compatible solutes proline, glycine betaine, and ectoine under conditions of high osmolality. Uptake of proline is mediated by both a high-affinity and a low-affinity secondary transport system. The low-affinity uptake system also accepts glycine betaine and ectoine as substrates. In the present study, the gene encoding the high-affinity proline uptake system PutP was isolated by heterologous complementation of Escherichia coli mutant strain WG389, which lacks the transport systems BetT, PutP, ProP, and ProU and is unable to synthesize proline and glycine betaine. This gene (putP) encodes a protein of 524 amino acids that shares identity with the proline transport systems PutP of E. coli, Staphylococcus aureus, Salmonella typhimurium, Haemophilus influenzae, and Klebsiella pneumoniae. Functional studies of PutP synthesized in E. coli mutant strain MKH13, which also lacks the transport systems for compatible solutes and is unable to synthesize glycine betaine, revealed that this carrier system is not regulated by the external osmolality on the level of activity. K m values of 7.6 mM for proline and 1.3 mM for sodium as cotransported ion were determined. Deletion of the putP gene allowed the functional characterization of another proline uptake system with low affinity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050480
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  • 9
    Electronic Resource
    Electronic Resource
    Urea uptake and urease activity in Corynebacterium glutamicum (1998)
    Springer
    Archives of microbiology 169 (1998), S. 411-416 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsCorynebacterium glutamicum ; Urea uptake ; Secondary transport ; Urease activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When Corynebacterium glutamicum is grown with a sufficient nitrogen supply, urea crosses the cytoplasmic membrane by passive diffusion. A permeability coefficient for urea diffusion of 9 × 10–7 cm s–1 was determined. Under conditions of nitrogen starvation, an energy-dependent urea uptake system was synthesized. Carrier-mediated urea transport was catalyzed by a secondary transport system linked with proton motive force. With a K m for urea of 9 μM, the affinity of this uptake system was much higher than the affinity of urease towards its substrate (K m approximately 55 mM urea). The maximum uptake velocity depended on the expression level and was relatively low [2–3.5 nmol min–1 (mg dry wt.)–1].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050591
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  • 10
    Electronic Resource
    Electronic Resource
    Effects of side-chains ofN-acetylamino acids on the structures of their triphenyltin(IV) complexes (1999)
    Springer
    Journal of radioanalytical and nuclear chemistry 241 (1999), S. 313-322 
    Details
    ISSN: 1588-2780
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract Triphenyltin(IV) complexes ofN-acetylglycine,N-acetyl-L-leucine,N-acetyl-L-asparagine andN-acetyl-L-tyrosine were prepared by two methods and characterized by means of different spectroscopic methods (FTIR, multinuclear,1H,13C and119Sn NMR and119Sn Mössbauer). The spectroscopic data indicated that theN-acetylglycine complex adopts a trigonal-bipyramidal structure in which the monodentate carboxylate and the amide-C=O group are bound to the same organotin(IV) moiety. The other three complexes are linear oligomers in which the planar Ph3Sn(IV) is coordinated axially by a monodentate carboxylate and an amide-C=O from two different ligands. At theC-terminal end of the oligomer chain there is a tetracoordinated tin(IV) with a monodentate carboxylate as donor group.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02347467
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