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  • 1
    ISSN: 0935-9648
    Keywords: Sensors ; ISFETs and CHEMFETs ; Polysiloxanes ; Reference FETs ; Polymer Membranes ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Synthetic receptor molecules that selectively bind charged guests can store chemical information. The transduction of this information into electronic signals connects the chemical and electronic domains. Field effect transistors (FETs) are attractive transducing elements because these microdevices are able to register and amplify chemical changes at the gate oxide surface of the semiconductor chip.Integration of molecular receptors and field effect transistors into one chemical system gives a device that can communicate-changes of substrate activities in aqueous solution. Simulations of a system in which the receptor molecules are directly attached to the FET gate oxide indicate serious limitations with respect to sensitivity, dynamic range and extreme requirements for complex stability. Therefore we have concentrated on the integration of covalently attached thin membranes.The problem of the thermodynamically ill-defined oxidemembrane ipterface has been solved by applying a covalently linked hydrophilic polyhydroxyethylmethacrylate (polyHEMA) gel between the sensing membrane and the silylated gate oxide. A buffered aqueous electrolyte solution in the hydrogel renders the surface potential at the gate oxide constant via the dissociation equilibrium of the residual silanol groups. The subsequent attachment of a polysiloxane membrane that has the required dielectric constant, glass transition temperature Tg, and receptor molecule, provides a stable chemical system that transduces the complexation of cationic species into electronic signals (CHEMFET).The response to changing K⊕ concentrations in a solution of 0.1 M NaCl is fast (〈1 sec) and linear in the concentration range of 10-5-1.0 M (55-58 mV /decade). A reference FET (REFET) based on the same technology is obtained when the intrinsic sensitivity to changes in ion concentration is eliminated by the addition of 2.10-5 mol g-1 of didodecyldimethyl ammonium bromide to the ACE membrane. Differential measurements with a REFET/CHEMFET combination showed excellent linear K⊕ response over long periods of time.All chemical reactions used are compatible with planar IC technology and allow fabrication on wafer scale.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 92 (1980), S. 429-444 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Glykogen-Phosphorylasen katalysieren den Abbau von Glykogen durch Phosphat (oder Arsenat) zu Glucose-1-phosphat (bzw. Glucose + Arsenat). Alle Glykogen-Phosphorylasen enthalten Pyridoxal-5′-phosphat, ein Vitamin-B6-Derivat, als Cofaktor. Es ist im Enzym durch eine Doppelbindung mit der ∊-Aminogruppe eines Lysinrestes verbunden. Wird der Cofaktor vom Enzymprotein abgetrennt, erhält man inaktives Apoenzym. Das Enzym bleibt jedoch aktiv, wenn man die Doppelbindung mit NaBH4 reduziert. Sollte daher Pyridoxalphosphat an der Katalyse der Glykogen-Phosphorylasen beteiligt sein, so müßte es eine andere Funktion als in allen anderen „klassischen“ Pyridoxalphosphat-abhängigen Enzymen haben, denn diese werden durch Reduktion inaktiviert. Die 31P-NMR-Spektroskopie hat gezeigt, daß die Phosphatgruppe von Pyridoxalphosphat in den katalytisch aktiven Formen der Glykogen-Phosphorylasen als Dianion in einer hydrophoben Umgebung vorliegt. Die kovalente und allosterische Aktivierung der Muskel-Glykogen-Phosphorylasen wird von der Umwandlung der monoprotonierten Form der Phosphatgruppe des Cofaktors in die dianionische Form begleitet. Wir fanden nun derartige Ionisierungsänderungen auch bei den nichtregulierten aktiven Kartoffel- und E. -coli-Maltodextrin-Phosphorylasen, und zwar bei der Bindung von Glucose und Oligosacchariden sowie bei katalytischem Umsatz, d. h. Arsenolyse der α-1,4-glykosidischen Bindungen. (Maltodextrin-Phosphorylasen gehören wie Glykogen-Phosphorylasen zur Klasse der α-Glucan-Phosphorylasen.) Versuche unserer Gruppe sowie neuere Befunde über die Raumstruktur der kristallinen Muskel-Glykogen-Phosphorylase legen es nahe, die dianionische Phosphatgruppe als Protonenacceptor beim Glucosyltransfer vom und zum Glucosylacceptor anzusehen. Wenn dies auch nicht die einzige Erklärung der Befunde sein mag, so kann doch nicht mehr daran gezweifelt werden, daß die dianionische Phosphatgruppe des Cofaktors der Glykogen-Phosphorylasen eine katalytische Funktion ausübt.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 95 (1983), S. 336-337 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 19 (1980), S. 441-455 
    ISSN: 0570-0833
    Keywords: Pyridoxal phosphate ; Enzyme catalysis ; Glycogen phosphorylases ; Phosphorylases ; Enzymes ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Glycogen phosphorylases catalyze the degradation of glycogen by phosphate (or arsenate) to glucose 1-phosphate (or glucose + arsenate). All glycogen phosphorylases that have been studied so far contain pyridoxal 5′-phosphate, a vitamin B6-derivative, as cofactor. Removal of the cofactor results in an inactive apoenzyme. However, reduction of the azomethine bond linking pyridoxal phosphate to an ε-aminolysyl side chain of the enzyme with NaBH4 does not inactivate glycogen phosphorylase. If therefore the cofactor should be involved in catalysis in glycogen phosphorylase it must function differently from all other classical pyridoxal phosphate dependent enzymes, for these are inactivated by reduction. 31P-NMR spectroscopy has revealed that the 5′-phosphate group of pyridoxal phosphate is present in catalytically active forms of glycogen phosphorylases as dianion in a hydrophobic environment shielded from aqueous solvent. Covalent and/or allosteric activation of muscle glycogen phosphorylases is accompanied by a transition of the monoprotonated form to the dianionic form of the phosphate group of the cofactor. We now report on such ionization changes in unregulated active potato- and E. coli maltodextrin phosphorylases on binding of glucose and oligosaccharides and following catalytic turnover, i.e. arsenolysis of α-1,4-glycosidic bonds. (Like glycogen phosphorylases, maltodextrin phosphorylases belong to the class of α-glucan phosphorylases.) The results of experiments carried out by our group together with recent findings on the three dimensional structure of crystalline muscle glycogen phosphorylases indicate a participation of the dianionic phosphate group as proton acceptor for the glucosyl transfer to and from the glucosyl acceptor. Although other interpretations are not excluded, at present little doubt remains that in the case of glycogen phosphorylases the dianionic phosphate group of the cofactor functions in catalysis.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Angewandte Chemie International Edition in English 22 (1983), S. 168-170 
    ISSN: 0570-0833
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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