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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    FEBS Letters 271 (1990), S. 236-238 
    ISSN: 0014-5793
    Keywords: Cell culture ; Compartmentation ; Geranyl pyrophosphate synthase ; Monoterpene synthesis ; Prenyltransferase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 57 (1992), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Residual pectin methylesterase activity (60% of initial activity) was present in cherry fruit stored 12 mo in brine. The specific activity of pectin methylesterase increased during the first 4 mo (195% of initial specific activity) but remained relatively stable thereafter. Methanol concentration increased (+144.5%) indicating that pectic substances underwent continuous demethylation during 12 mo storage. Pectin deesterification was probably of enzymatic origin since notable chemical deesterification occurred only at a pH lower than that found in fruit during storage. Residual pectin methylesterase activity introduces the possibility of improving fruit texture by manipulating physico-chemical conditions prior to blanching and candying.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Plant cell reports 1 (1982), S. 91-93 
    ISSN: 1432-203X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cell suspension cultures of “Muscat de Frontignan” grapes Vitis vinifera L. are able to convert citral (a mixture of neral and geranial) into the corresponding monoterpenic alcohols, nerol and geraniol. The geraniol formed is esterified into geranyl acetate. Bioconversion of nerol or geraniol added alone to the cell suspension was also studied. Interconversions between these different monoterpenic compounds are described and discussed.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-2048
    Keywords: Carrier (plastid envelope) Isopentenyl diphosphate ; Plastid (uptake experiments) ; Vitis (cell suspensions)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The uptake of [1-14C]isopentenyl diphosphate by intact plastids purified from cell suspensions of Vitis vinifera L. cv. Muscat de Frontignan was investigated using vacuum-filtration and silicone-oil-filtering techniques. Transport across the plastid envelope which was stimulated by cations, such as Mg2+ and Mn2+, was characterized by a K m of approx. 0.5 mM and a V max of 25 nmol·(mg protein)-1·-h-1. The data showed that isopentenyl diphosphate apparently accumulated in the plastid against a concentration gradient. The involvement of a protein carrier was suggested by the strong inhibition of the uptake by compounds which are known to block SH groups. Thus, the saturation kinetics together with the pH optimum (7.5–8), the temperature dependence (maximum incorporation at 37 °C) and the competitive inhibition by a structural analogue of the substrate (aminophenylethyl diphosphate) provided evidence for a mechanism of uptake by facilitated diffusion. The carrier identified may thus play a major role in supplying the plastid compartment with isopentenyl diphosphate for isoprenoid biosynthesis.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-2048
    Keywords: Cell culture (enzyme localization) ; Geranyl diphosphate synthase ; Monoterpene ; Plastid (monoterpene synthesis) ; Vitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Intact plastids from cell suspensions of Vitis vinifera L. cv. Muscat de Frontignan, free of detectable contamination by other particles as judged by the distribution of organelle-specific marker enzymes and by electron microscopy, exhibit geranyl-diphosphate synthase activity (EC 2.5.1.1). This synthase activity remains stable after tryptic digestion of unlysed organelles and is enhanced by plastid disruption. We conclude that the enzyme is located within the organelle. The possibility of an isopentenyl diphosphate/dimethylallyl diphosphate translocating system which would play a major role in the regulation of monoterpene metabolism is discussed.
    Type of Medium: Electronic Resource
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