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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 39 (1983), S. 926-928 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A slide latex test for detection of anti-zona pellucida activity in human sera was developed using a latex agglutination reaction. The latex reagent, made of polystyrene particles coated with solubilizing zona antigen(s), was found to give results comparable in sensitivity as well as specificity to those of the indirect immunofluorescence method as tested with anti-pig-zona antiserum and with human sera. Thus, the slide latex test was judged to be adequate for use instead of the indirect immunofluorescence technique.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Development genes and evolution 207 (1997), S. 194-198 
    ISSN: 1432-041X
    Keywords: Key words Fluorescent probes ; In situ hybridization ; Distal-less ; Imaginal disc ; Confocal microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We report a new technique using fluorescent probes to detect a mRNA and a protein simultaneously in the Drosophila embryo. For in situ hybridization, 3-hydroxy-N-2′-biphenyl-2-naphthalenecarboxamide phosphate ester (HNPP)/Fast Red TR was used as a fluorescent substrate for alkaline phosphatase. It was possible to compare protein and mRNA expression on a cell by cell basis with a laser scanning confocal microscope. We applied this technique to analyse the dynamics of Distal-less (Dll) enhancer activity in the thoracic limb primordium in the early Drosophila embryo. We stained embryos bearing the Dll early enhancer (Dll-304) fused to the Escherichia coli lacZ gene. LacZ mRNA was detectable in the ventral region of the limb primordium, and β-galactosidase protein in the dorsal region. In the middle, both mRNA and protein were detectable. These results suggest that the Dll enhancer is activated in the ventral region of the limb primordium and that Dll-positive cells migrate from a ventral position to a dorsal one within a single limb primordium.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 26 (1970), S. 347-348 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Isolierung und Strukturaufklärung eines neuen Sesquiterpenalkohols ausBazzania pompeana (Lac.) Mitt.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Streptococcus mutans ; Glucosyltransferase ; Fructosyltransferase ; Electrophoresis ; Isoelectric focussing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Streptococcus mutans was classified by the electrophoretic properties of glucosyltransferases (GTases) and fructosyltransferases (FTases). The cells of serotypes a, d and g did not release extracellular FTases, although those from other serotypes did. The enzymes from cells of serotypes d and g synthesized a good deal of insoluble polysaccharide compared with other serotypes. The enzymes were applied to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), and polyacrylamide gel-isoelectric focussing (PAG-IEF). Gels were stained for their activity and protein content. Enzymes belonging to the same serotype gave the same specific pattern on both gels. The seven serotypes could be classified into the following four groups: serotypes d and g, serotype a, serotypes c, e and f, and serotype b. The results agree well with some previous reports based on other methods. The molecular weights of three GTase bands were 156K, 146K and 135K, and of four kinds of FTase bands were 108K, 95K, 80K and 76K. The isoelectric points of main enzymes were 4.25, 4.60, 5.00, 5.55 and 5.70. Those of FTases were 4.25 and 4.60.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of materials science 8 (1989), S. 505-506 
    ISSN: 1573-4811
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of materials science 9 (1990), S. 382-385 
    ISSN: 1573-4811
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 7 (1991), S. 522-525 
    ISSN: 1573-0972
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Sucrose at 10 to 20% (w/v) was the best carbon source for the production of β-fructofuranosidase by Aureobasidium sp. ATCC 20524. At higher concentrations, it arrested growth. Glucose and fructose were also good carbon sources for the enzyme production. Yeast extract at 1.5 to 2% (w/v) was the best nitrogen source for the enzyme production and for cell growth. Addition of NaNO3 (1 to 2%, w/v) and MgSO4·7H2O (0.5 to 1.5%, w/v) to the cultivation medium increased the intracellular enzymatic activity. The total enzymatic activity and cell growth reached 1.2×104 U/flask and 2.5 g dry cell/flask, respectively after 48 h.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 8 (1992), S. 155-159 
    ISSN: 1573-0972
    Keywords: Aspergillus ; enzyme production ; fructofuranosidase ; sucrose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A newly isolated strain, MU-2, which produces very high β-fructofuranosidase activity, was identified asAspergillus japonicus. For enzyme production by the strain, sucrose at 20% (w/v) was the best carbon source and yeast extract at 1.5 to 3% (w/v) the best nitrogen source. Total enzymatic activity and cell growth were at maximum after 48 h, at 1.57×104 U/flask and 0.81 g dry cells/flask, respectively. The optimum pH value of the enzymatic reaction was between 5.0 and 5.5 and the optimum temperature 60 to 65°C. The enzyme produced 1-kestose (O-β-d-fructofuranosyl-(2→1)-β-d-fructofuranosyl α-d-glucopyranoside) and nystose (O-β-d-fructofuranosyl-(2→1)-β-d-fructofuranosyl-(2→1)-β-d-fructofuranosyl α-d-glucopyranoside) from sucrose by fructosyl-transferring activity. The strain was found to be very useful for industrial production of β-fructofuranosidase.
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 8 (1992), S. 276-279 
    ISSN: 1573-0972
    Keywords: Aspergillus japonicus ; β-fructofuranosidase ; glycoprotein ; 1-kestose ; nystose ; sucrose
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract β-Fructofuranosidase fromAspergillus japonicus, which produces 1-kestose (O-β-d-fructofuranosyl-(2→1)-β-d-fructofuranosyl α-d-glucopyranoside) and nystose (O-β-d-fructofuranosyl-(2→1)-β-d-fructofuranosyl-(2→1)-β-d-fructofuranosyl α-d-glucopyranoside) from sucrose, was purified to homogeneity by fractionation with calcium acetate and ammonium sulphate and chromatography with DEAE-Cellulofine and Sephadex G-200. Its molecular size was estimated to be about 304,000 Da by gel filtration. The enzyme was a glycoprotein which contained about 20% (w/w) carbohydrate. Optimum pH for the enzymatic reaction was 5.5 to 6. The enzyme was stable over a wide pH range, from pH 4 to 9. Optimum reaction temperature for the enzyme was 60 to 65°C and it was stable below 60°C. The Km value for sucrose was 0.21m. The enzyme was inhibited by metal ions, such as those of silver, lead and iron, and also byp-chloromercuribenzoate.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 9 (1993), S. 216-220 
    ISSN: 1573-0972
    Keywords: Aspergillus ; β-fructofuranosidase ; fructo-oligosaccharide ; immobilization ; porous silica
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract β-Fructofuranosidase from Aspergillus japonicus MU-2, which produces fructo-oligosaccharides (1-kestose: O-β-D-fructofuranosyl-(2 → 1)-β-D-fructofuranosyl α-D-glucopyranoside); and nystose: O-β-D-fructofuranosyl-(2 → 1)-β-D-fructofuranosyl-(2 → 1)-β-D-fructofuranosyl α-D-glucopyranoside) from sucrose, was immobilized, covalently with glutaraldehyde onto alkylamine porous silica, at high efficiency (64%). Optimum pore diameter of porous silica for immobilization of the enzyme was 91.7 nm. After immobilization, the enzyme's stabilities to temperature, metal ions and proteolysis were improved, while its optimum pH and temperature were unchanged. The highest efficiency of continuous production of fructo-oligosaccharides (more than 60%), using a column packed with the immobilized enzyme, was obtained at 40% to 50% (w/v) sucrose. The half-life of the column during long-term continuous operation at 55°C was 29 days.
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