On-Chip Generation, Routing, and Detection of Resonance Fluorescence.

Quantum optical circuits can be used to generate, manipulate, and exploit nonclassical states of light to push semiconductor based photonic information technologies to the quantum limit. Here, we report the on-chip generation of quantum light from individual, resonantly excited self-assembled InGaAs quantum dots, efficient routing over length scales ≥1 mm via GaAs ridge waveguides, and in situ detection using evanescently coupled integrated NbN superconducting single photon detectors fabricated on the same chip. By temporally filtering the time-resolved luminescence signal stemming from single quantum dots we use the quantum optical circuit to perform time-resolved excitation spectroscopy on single dots and demonstrate resonance fluorescence with a line-width of 10 ± 1 µeV; key elements needed for the use of single photons in prototypical quantum photonic circuits.

[Kaspar Schwenckfeldt--a Silesian physician, Renaissance student of nature, and bibliophile]. / Kaspar Schwenckfeldt--slaski lekarz, renesansowy badacz przyrody i bibliofil.

Kaspar Schwenckfeldt (1563-1609) is numbered among the intellectual celebrities of the Age of Renaissance in Silesia. He was the first to describe the flora of this region. His work Stirpium et fossilium Silesiae catalogus, based on his own research, was the fundamental source of knowledge about those plants for almost two centuries. His work on Silesian mineralogy, Fossilium Silesiae catalogus, omnia generis mineralia, metalla, succos, terrae, lapillos, fontes medicatos et thermae continens, even at present day is a valuable source of information on the occurrence of minerals in Silesia in the distant past. On the basis of Theriothropeum Silesiae one can reconstruct the rich realm of Silesian fauna of 16th/17th centuries. The monography of cieplice Slaskie, Hirschbergischen warmen Bades, published in 1607, is one of the oldest descriptions of this spa. The analysis of the physical-chemical characteristics of the waters and the information about their possible medical application was the fullest expert's opinion of that time. Up to the present days, a hand-written register of his collection of books has been preserved in the Stadtarchiv in Görlitz. It contains 705 items, which include medical publications, works on magic and occultism, as well as books connected with the Reformation movement, studies in Old Greek and Latin philologies, books on the history of some European countries. His versatility and rich scientific output place him among the most outstanding minds of his age.

[Enzymes catalyzing the reduction of aldopentoses and the oxidation of pentitols in Mycobacteria]. / Enzymes catalysant la réduction des aldopentoses et l'oxydation des Pentitols chez les Mycobactéries.

M. phlei, grown on synthetic Sauton medium (with 6% glycerol as carbon source), had NADPH- and NADH-aldopentose reductase, as well as NAD-pentitol dehydrogenase activities; some of their properties are studied. These activities are not present in BCG grown on the same medium. All experiments of aldopentose-reductase induction in BCG on a D(+)xylose medium were negative.

[Dehydrogenases reducing NAD+ in the presence of D (-) 3- phosphoglycerate in mycobacteria (BCG, H37Ra, M. phlei)]. / Déshydrogénases réduisant le NAD+ en présence du D (-) 3-phosphoglycérate chez les mycobactéries (BCG, H37Ra, M. phlei).

Referring to the elution volume on a Sephadex G-150 column only one specific peak is obtained, the same for the BCG, H37Ra and Mycobacterium phlei strains grown on Sauton synthetic medium. Some properties of these partially purified dehydrogenases are studied (conservation and dialysis in media of different salt concentrations, equilibrium constant, Km, heat stability). All enzyme preparations from tubercle bacilli (BCG, H37Ra) are readily inactivated by heat and are very unstable in solutions of low ionic strength. In contrast, under the same experimental conditions, all enzyme samples from M. phlei are, comparatively, much more stable towards these factors [heat, salt (potassium phosphate, NaCl) concentration].

[Polyol dehydrogenases in mycobacteria (author's transl)]. / Polyol-déhydrogénases des mycobactéries.

Contrary to the the tubercle bacilli (H37Ra, BCG), Mycobacterium phlei, grown on Sauton medium, formed the NAD+ dependent dehydrogenases that catalyse the oxidation of ribitol, sorbitol and mannitol. These enzymes were separated by chromatography on DEAE-cellulose and Sephadex G-200. In the present work we have principally studied the ribitol dehydrogenase. All the experiments for induction of the ribitol dehydrogenase in H37Ra or BCG were negative; whereas after the adaptation of M. phlei to ribitol, the specific activity of this enzyme increased in the supernatants more than 100 per cent. The ribitol dehydrogenase of M. phlei reduced NAD+ not only in the presence of ribitol but also (though to a lesser extent) in the presence of erythritol and glycerol. Other properties studied concerning this enzyme and the reaction it catalyses were: pH dependence, equilibrium constant, Km and sensitivity towards the inhibitors of the thiol groups.

[Enzymatic differences in mycobacteria. Ribitol dehydrogenase]. / Différences enzymatiques chez les mycobactéries. Ribitol déshydrogénase.

Contrary to the tubercle Bacilli (H37Ra, BCG), Mycobacterium phlei has a ribitol-NAD dehydrogenase (that also oxidizes, although to a lesser extent, erythritol and glycerol). This difference is observed with the Bacteria grown on Sauton's medium, as well as after their adaptation to ribitol. The extracts of all these Mycobacteria reduce, NADP in the presence of glycerol, ribitol or erythritol, though very slowly.

[Asparagine metabolism in mycobacteria. II. -- Asparagine hydrolysis and aspartohydroxamic acid formation and hydrolysis catalysed by M. fortuitum, M. phlei and BCG asparaginases (author's transl)]. / Metabolisme de l'asparagine chez les mycobactéries. II.--Hydrolyse de L'Asparagine, Formation et Hydrolyse de L'Acide Aspartohydroxaminique catalysées par les asparaginases de M. fortuitum, de M. phlei et du BCG

Crude extracts of BCG, M. fortuitum and M. phlei, hydrolyse asparagine (I) and L-beta-asparthohydroxamic acid (III), and catalyse the synthesis of aspartohydroxamic acid from asparagine and hydroxylamine (II). The ratio between these enzymatic activities (I:II and I:III) presents a certain stability during the different steps of purification of these mycobacteria asparaginases. In particular, M. fortuitum asparaginase has been purified 90 to 130-fold, with recovery of approximately 10%. Only the fractions of supernatants which have an asparaginase activity catalyse the formation of aspartohydroxamate from asparagine and hydroxylamine. Some differences between the asparaginases of these strains are described. Particularaly, in comparison to reaction I, their abilities to catalyse reactions II and III vary noticeably from one asparaginase to an other. The asparaginase of BCG catalyses very slightly in the reactions II and III and is more specific of L-asparagine hydrolysis than are the asparaginases of M. fortuitum and of M. phlei. Furthermore, in the case of M. phlei, p-chloromercuribenzoate (pCMB) inhibits very stronly the reactions I and III and slightly reaction II, whereas conversely, for M. fortuitum, pCMB does not inhibit reactions I and III but strongly inhibits reaction II. In the case of BCG, these three reactions are not inhibited by pCMB. Moreover, the asparaginases from these strains are more or less sensitive to the ionic strength of the buffer used.