ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Collection
Keywords
Publisher
Years
  • 1
    facet.materialart.
    Unknown
    Meteorological measurements in the upper air at station Friedrichshafen, 1929-09-07 to 1930-03-16, ERA-CLIM ID 5557
    PANGAEA
    Details
    Publication Date: 2023-05-12
    Keywords: ALTITUDE; DATE/TIME; ERA-CLIM; ERA-CLIM_5557; European Reanalysis of Global Climate Observations; Friedrichshafen; Germany; Weather station/meteorological observation; Wind direction; Wind speed; WST
    Type: Dataset
    Format: text/tab-separated-values, 526 data points
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    DATA PANGAEA
  • 2
    facet.materialart.
    Unknown
    Meteorological measurements in the upper air at station Arosa, 1929-09-08 to 1930-03-16, ERA-CLIM ID 5556
    PANGAEA
    Details
    Publication Date: 2023-05-12
    Keywords: ALTITUDE; Arosa; DATE/TIME; ERA-CLIM; ERA-CLIM_5556; European Reanalysis of Global Climate Observations; Switzerland; Weather station/meteorological observation; Wind direction; Wind speed; WST
    Type: Dataset
    Format: text/tab-separated-values, 593 data points
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    DATA PANGAEA
  • 3
    Electronic Resource
    Electronic Resource
    L'ozono atmosferico alle latitudini elevate (1942)
    Springer
    Pure and applied geophysics 4 (1942), S. 103-105 
    Details
    ISSN: 1420-9136
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences , Physics
    Description / Table of Contents: Zusammenfassung Auf Grund der neueren Beobachtungen erläutert der Verf. die jahreszeitlische Verteilung des atmosphärischen Ozonbetrages in Funktion der geographischen Breite.
    Notes: Riassunto In base alle più recenti osservazioni, l'A. illustra graficamente e discute l'andamento stagionale della quantità di ozono nell'atmosfera in funzione della latitudine geografica.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02112100
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cloning, sequencing, and characterization of a gene (narT) encoding a transport protein involved in dissimilatory nitrate reduction in Staphylococcus carnosus (1997)
    Springer
    Archives of microbiology 166 (1997), S. 361-367 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsStaphylococcus carnosus ; Tn917 insertion mutant ; Nitrate uptake ; Nitrite export
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A Tn917 mutant of Staphylococcus carnosus TM300, nrIII, was isolated and characterized. Mutant nrIII did not take up nitrate or accumulate nitrite when grown in B-medium supplemented with up to 10 mM nitrate under anoxic conditions; however, it displayed wild-type levels of benzyl Δ viologen-linked nitrate reductase activity. Cultivated in B-medium with nitrate under oxic conditions, mutant nrIII accumulated fivefold less nitrite than the wild-type. The mutation in S. carnosus nrIII could be complemented with a 2-kb chromosomal EcoRI-HpaI fragment from the wild-type. The gene affected by transposon insertion in mutant nrIII was cloned and sequenced. Analysis of the deduced amino acid sequence revealed that this gene, designated narT, encodes a highly hydrophobic 42-kDa transmembrane protein of 388 amino acids and shows similarities to transport proteins that play a role in nitrate import or nitrite export. The inability of nrIII to take up nitrate under anoxic conditions and its ability to take up and accumulate nitrite in the presence of benzyl viologen, a nitrate ionophore, under the same conditions suggest that NarT represents a transport protein required for nitrate uptake under anoxic conditions in S. carnosus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01682980
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Characterization of the molybdate transport system ModABC of Staphylococcus carnosus (1999)
    Springer
    Archives of microbiology 172 (1999), S. 109-115 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsStaphylococcus carnosus ; Nitrate ; reductase ; Tn917 insertion mutants ; Molybdate ; transport ; Molybdenum cofactor biosynthesis ; Lipoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Transposon mutagenesis of Staphylococcus carnosus led to the identification of three genes, modABC, which encode an ABC transporter that is involved in molybdate transport. It was shown by [14C]palmitate labeling that ModA represents a lipoprotein that in gram-positive bacteria is the counterpart of the periplasmic binding proteins of gram-negative organisms. The sequence characteristics identify ModB as the integral-membrane, channel-forming protein and ModC as the ATP-binding energizer for the transport system. Mutants defective in modABC had only 0.4% of the wild-type nitrate reductase activity. Molybdate at a non-physiologically high concentration (100 μM) fully restored nitrate reductase activity, suggesting that at least one other system is able to transport molybdate, but with lower affinity. The expression of modA (and most likely of modBC) was independent of oxygen and nitrate. To date, there are no indications for molybdate-specific regulation of modABC expression since in a modB mutant, modA expression was unchanged in comparison to the wild-type.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050747
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Chemical and biochemical studies for the differentiation of coagulase-positive staphylococci (1976)
    Springer
    Archives of microbiology 110 (1976), S. 263-270 
    Details
    ISSN: 1432-072X
    Keywords: Coagulase-positive staphylococci ; Cell wall composition ; Lactic acid configuration ; FDP-activatedl-LDH ; Esterase pattern ; Staphylococcus aureus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cell wall composition, the configuration of lactic acid produced from glucose under anaerobic conditions, the occurrence of fructose-1,6-diphosphate (FDP) activatedl-lactate dehydrogenase (l-LDH), and the esterase pattern were determined from more than 80 strains of coagulase-positive staphylococci isolated from man and animal. Strains isolated from man, swine, bovines and hares form a rather homogencous group. They exhibit a similar cell wall composition, produce predominantlyd,l-lactate and have a characteristic and simple esterase pattern. Coagulasepositive staphylococci isolated from dogs, horses, minks and pigeons are quite distinct from typicalStaphylococcus aureus strains. They exhibit a different cell wall composition, produce onlyl-lactate, possess anl-LDH which is specifically activated by FDP, and have a quite complex esterase pattern.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690237
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Oxygen utilization by Lactobacillus plantarum (1980)
    Springer
    Archives of microbiology 125 (1980), S. 209-214 
    Details
    ISSN: 1432-072X
    Keywords: NAD(P)H oxidase ; Pyruvate oxidase ; Lactate oxidase ; NADH peroxidase ; Lactobacillus plantarum ; Lactic acid bacteria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Lactobacillus plantarum (ATCC 8014) cells, grown aerobically on glucose medium, consumed molecular oxygen when incubated with either glucose, d/l-lactate or pyruvate as substrate. Cell extracts catalyzed the oxidation of NADH, d/l-lactate or pyruvate with O2. Per mol O2 2mol of NADH were consumed indicating that O2 was reduced to H2O; reduction proceeded via H2O2 involving a NADH oxidase and a NADH peroxidase. Catalase activity was absent. Pyruvate oxidation with O2 led to the formation of H2O2, lactate oxidation to the formation of H2O. Thus in L. plantarum different mechanisms are available by which molecular oxygen can be used as electron acceptor for oxidation reactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446878
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Oxygen utilization by Lactobacillus plantarum (1980)
    Springer
    Archives of microbiology 125 (1980), S. 215-220 
    Details
    ISSN: 1432-072X
    Keywords: Lactobacillus plantarum ; Superoxide dismutase ; Superoxide anion ; Pulse radiolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell-free extracts of Lactobacillus plantarum contain non-proteinaceous compounds which mimic superoxide dismutase activity. Using the test system in which O 2 − is generated by xanthine oxidase, superoxide dismutase activity is found in cell-free extracts, where proteins are removed by precipitation. This activity is strongly decreased after dialysis of cell-free extracts. Superoxide dismutase activity was also investigated by means of pulse radiolysis. Cell-free extracts of Escherichia coli were also investigated as a comparison, which were known to contain superoxide dismutase. With cell-free extracts of both L. plantarum and E. coli the decay of O 2 − was markedly increased. However, the type of reaction of the O 2 − decay was of first order in the presence of E. coli extracts due to superoxide dismutase(s), and of second order in the presence of L. plantarum extracts, indicating that O 2 − elimination is not an enzymic reaction. Mn2+ phosphate(s) might be responsible for the observed elimination of O 2 − . The production of O 2 − is not detectable during NADH-, lactate- or pyruvate oxidase reactions in L. plantarum extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446879
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Distribution of superoxide dismutases, oxidases, and NADH peroxidase in various streptococci (1984)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 21 (1984), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Managanese-containing superoxide dismutase and NADH oxidase could be detected in all of the 23 strains belonging to different species or serotypes of the genus Streptococcus. NADH peroxidase activity was found in 7 strains. Pyruvate oxidase activity was only detectable in Streptococcus faecalis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1984.tb00218.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Occurrence of d-tagatose-6-phosphate pathway of d-galactose metabolism among staphylococci (1978)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 3 (1978), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1978.tb01873.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...