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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Phytochemistry 20 (1981), S. 379-382 
    ISSN: 0031-9422
    Keywords: Gramineae ; Triticum vulgare ; cold hardiness ; electrophoresis. ; esterases ; leaf ; protein ; wheat
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Phytochemistry 26 (1986), S. 149-153 
    ISSN: 0031-9422
    Keywords: M,s ; Palmae ; Phoenix dactylifera ; dates ; electrophoresis. ; isoelectric points ; protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Fresenius' Zeitschrift für analytische Chemie 263 (1973), S. 27-32 
    ISSN: 1618-2650
    Keywords: Esterase ; in Polyacrylamidgel inkludierte Kartoffelesterase ; Elektrophorese, Gel ; Inklusion von Kartoffelesterase in Polycrylamidgel
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Summary An isoenzyme of potato esterase has been entrapped in situ after polyacrylamide (PAA)-electrophoresis, using PAA of different concentrations and crosslinking. Best results in respect to diffusion, flow rates and yield (77%) have been found for a gel containing 6% acrylamide with 6% methylen-bis-acrylamide, penetrating a gel of cyanogum with esterase. The latter is stabilized during polymerization by the gel. Properties of the entrapped enzyme (pHi, K m, MW etc.) have been determined, 100 fold better storage stability is achieved.
    Notes: Zusammenfassung Von den Kartoffelesterasen wurde ein Isoenzym durch Gel-Elektrophorese in Polyacrylamid (PAA) getrennt. Das entsprechende Gelstück mit dem durch das Netzwerk stabilisierten Enzym tränkte man mit AA und Vernetzer (BIS) unterschiedlicher Konzentration und polymerisierte mit Licht das Enzym ein. Die Mischungen AA/BIS sind in einem bestimmten Verhältnis (6∶0,36) optimal., eine Ausbeute von 77% der Anfangsaktivität kann erreicht werden. Einige Eigenschaften (pHi, K m, MG u.ä.) werden beschrieben, insbesondere ist die 100fach bessere Lagerstabilität hervorzuheben.
    Type of Medium: Electronic Resource
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