Publications by authors named "Haemmerli S"

From early infancy, humans reason about the external world in terms of identifiable, solid, cohesive objects persisting in space and time. This is one of the most fundamental human skills, which may be part of our innate conception of object properties. Although object permanence has been extensively studied across a variety of taxa, little is known about how non-human animals reason about other object properties.

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We have constructed 2-micron-based yeast expression vectors containing a copy of the metallothionein (CUP1) gene of Saccharomyces cerevisiae as a semi-dominant, selectable marker. When used for the expression of the thrombin inhibitor hirudin, originally derived from the leech Hirudo medicinalis, these vectors displayed the following characteristics. (1) In the presence of copper salts, they were mitotically more stable than similarly designed control vectors lacking the CUP1 gene.

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Fibre-optic biosensors were constructed for determination of hypoxanthine and xanthine. Xanthine oxidase and peroxidase were immobilized on different preactivated membranes which were subsequently mounted onto the tip of a fibre-optic bundle. The H2O2 generated by the reaction of hypoxanthine and xanthine oxidase was measured by chemiluminescence (CL) detection using luminol and peroxidase.

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A new kind of calorimetric biosensor for the measurement of the heat (molar enthalpy change) of enzymatic reactions is presented. The device operates according to the Seebeck effect, the same principle on which thermocouples are based. The thermopile used in this work consists of an array of p-type silicon/aluminium strips integrated on a thin silicon membrane (5 microns).

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Miniaturization will unify the different approaches chosen for the application of biosensors in bioprocess control. The most versatile system, which in our opinion is flow injection analysis will be the method of choice for the introduction of biosensors in bioprocess control. A lot of experience will be gained for the future development of miniaturized total chemical analysis systems.

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Benzo(a)pyrene was oxidized with crude and purified extracellular ligninase preparations from Phanerochaete chrysosporium. Both the crude enzyme and the purified fractions oxidized the substrate to three organic soluble products, namely benzo(a)pyrene 1,6-, 3,6-, and 6,12-quinones. These findings support the recent proposition that lignin-degrading enzymes are peroxidases, mediating oxidation of aromatic compounds via aryl cation radicals.

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