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  • Chemistry  (3)
  • Biochemistry and Biotechnology  (2)
  • Abbreviations: NAA: 1-naphthaleneacetic acid; BA: benzyladenine; MS: Murashige and Skoog (1962); GUS: β-glucuronidase (EC 3.2.1.31); NPT II: neomycin phosphotransferase (EC 2.7.1.95); NOS: nopaline synthase; CaMV: Cauliflower Mosaic Virus; CTAB: cetyl triethylammonium bromide; X-GLUC: 5-bromo-4-chloro-3-indolyl-β-D-glucuronide; PCR: polymerase chain reaction  (1)
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Material
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  • 1
    Electronic Resource
    Electronic Resource
    Genetic transformation of Begonia tuberhybrida by Ri rol genes (1996)
    Springer
    Plant cell reports 15 (1996), S. 606-609 
    Details
    ISSN: 1432-203X
    Keywords: Abbreviations: NAA: 1-naphthaleneacetic acid; BA: benzyladenine; MS: Murashige and Skoog (1962); GUS: β-glucuronidase (EC 3.2.1.31); NPT II: neomycin phosphotransferase (EC 2.7.1.95); NOS: nopaline synthase; CaMV: Cauliflower Mosaic Virus; CTAB: cetyl triethylammonium bromide; X-GLUC: 5-bromo-4-chloro-3-indolyl-β-D-glucuronide; PCR: polymerase chain reaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. We have developed an Agrobacterium-mediated transformation system for commercial Begonia species. The leaf explants of Begonia semperflorens, Begonia x hiemalis and B. tuberhybrida were inoculated with Agrobacterium tumefaciens LBA4404 harboring a binary vector pBI121 which contains rolA,B and C genes of an agropine type Ri plasmid (pRiA4b). Kanamycin resistant shoots of B. tuberhybrida were obtained on MS agar medium supplemented with 0.1 mg/l NAA, 0.5 mg/l BA, 500 mg/l claforan and 100 mg/l kanamycin. These shoots exhibited GUS activity and Southern analysis showed a single copy insertion into the genome. When the transgenic plants were transferred to soil, they displayed the phenotype specific to the transgenic plants by A. rhizogenes such as dwarfness, delay of flowering, and wrinkled leaves and petals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002990050083
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Rapid assay of β-galactosidase and sialyltransferase by lectin affinity high performance liquid chromatography with fluorescence detectionThis study was entrusted to the Hohen Oil Company Ltd, by the Science and Technology Agency (STA) using the Special Coordination Funds for Promoting Science and Technology. (1989)
    New York, NY : Wiley-Blackwell
    Biomedical Chromatography 3 (1989), S. 110-113 
    Details
    ISSN: 0269-3879
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Fluorescein isothiocyanate (FITC)-labelled asialotransferrin and pyridyl aminated oligosaccharides were prepared from asialotransferrin and human milk using affinity chromatography and high performance liquid chromatography (HPLC), respectively. These substances were incubated with galactosidase or sialyltransferase and then examined by lectin affinity HPLC. The elution patterns changed according to the period of incubation and amount of enzyme. This analytical method using lectin affinity HPLC with fluorescence labelled glycoprotein or oligosaccharides as the substrates has great value for detecting these enzyme under the same chromatographic conditions. In addition, differences were noted in the activity of β-galactosidase toward oligosaccharides having the Gal β(1 → 3)GlcNAc or Gal β(1 → 4)GlcNAc structure at reducing termini.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bmc.1130030304
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Increased selectivity in the detection of glycoproteins on nitrocellulose membranes by washing with sodium hydroxide solution (1991)
    Weinheim : Wiley-Blackwell
    Electrophoresis 12 (1991), S. 685-686 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: We increased selectivity in the detection of glycoproteins on nitrocellulose membranes by introducing a washing step using sodium hydroxide solution. Glycoproteins on the nitrocellulose membrane were first oxidized by sodium periodate; biotin hydrazide was then coupled to the aldehyde groups generated in the sugar moiety of the glycoproteins. The membrane was washed twice using sodium hydroxide solution, and avidin-horseradish peroxidase was then coupled to the remaining biotin. This system allows the detection of nanograms of glycoproteins on nitrocellulose membranes, and its specificity allows the clear distinction of glycoproteins from the nonglycosylated protein of bovine serum albumin.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150120918
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Estimation of biotinylated lectin by isoelectric focusing (1990)
    Weinheim : Wiley-Blackwell
    Electrophoresis 11 (1990), S. 505-506 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Concanavalin A (Con A) was biotinylated to various degrees using N-biotinyl-ω-aminocaproic-acid-N-hydroxy succinimide ester as the biotinylation reagent, and then analyzed by isoelectric focusing using PhastGel IEF 3-9. The isoelectric points of biotinylated ConAs were found to decrease with increasing concentration of the biotinylation reagent. Analysis by isoelectric focusing followed by dot blotting clearly indicated that the biotinylated ConA with an isoelectric point lower than that of the original ConA by 2.2 ± 0.6 had the strongest binding activity for ovalbumin.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150110613
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    Paper (German National Licenses)
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