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  • 1995-1999  (1)
  • 1980-1984  (1)
  • anthocyanin  (1)
  • electrochemistry  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Euphytica 32 (1983), S. 205-216 
    ISSN: 1573-5060
    Keywords: Rosa ; rose genetics ; flower pigments ; paper chromatography ; anthocyanin ; cyanin ; peonin ; pelargonin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary In breeding for color and winter hardiness in Rosa, more than 1200 progeny from 47 families were analyzed for anthocyanin pigments. Cyanin, peonin and pelargonin were found in 99%, 52% and 31% respectively, of the seedlings. Each pigment was highly heritable from seed or pollen parents or both. All showed quantitative inheritance, particularly cyanin and peonin. A system is proposed to explain most of the synthetic pathways and controls for anthocyanin production in roses.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 8 (1998), S. 101-105 
    ISSN: 1057-9257
    Keywords: biosensor ; protein immobilisation ; protein modification ; electrochemistry ; nitrotyrosine ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Use of electrosynthetic methodology allows the production of hen egg-white lysozyme (HEWL) either mononitrated at tyrosine 23 or bisnitrated at tyrosines 20 and 23, but never nitrated at tyrosine 53. This is a different sequence from that obtained by the chemical nitrating agent tetranitromethane, and when reduced by dithionite, the selectively modified enzyme can be anchored at pH 5 via the unique aromatic amino group to magnetic beads or other suitable matrices. HEWL so immobilised loses less than 10% of cell-wall lytic activity compared with the approximately 50% loss of activity when immobilised by conventional methodology at pH 9 via essentially random reaction at lysine residues and other functionalities which are nucleophilic at this pH. This result offers promise as a general method for selective protein immobilisation in biosensors and similar applications. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 1 Tab.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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