Technique d'inclusion et d'ultramicrotomie,destinée à l'étude du développement des organelles dans une cellule isolée

Summary (1) Control of cell orientation and knowledge of the plane of sectioning are indispensable (but generally ignored) requirements for studies of the development of cellular constituents. (2) A simple technique that meets these requirements for the electron microscope is given. (3) As applied toParamecium, it is shown that the ciliary complexes of the new gullet develop outside of the old one, and that invagination begins at the anterior end of the gullet anlage.

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Travail effectué dans le cadre d'une recherche faite en collaboration avec les Instituts d'Histologie et de Biophysique, grâce à une subvention de «Fritz Hoffmann-La Roche-Stiftung zur Förderung wissenschaftlicher Arbeitsgemeinschaften in der Schweiz».     

Mass fragmentographic determination of cholecalciferol and 25-hydroxycholecalciferol in human serum

Summary The serum extracts were purified by column-, thin layer- and high pressure liquid chromatography. Deuterated cholecalciferol and deuterated 25-hydroxycholecalciferol were used as internal standards. The quantitative analysis was performed using GC-mass fragmentography technique of TMS-ethers.     

Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase

Oxygen-evolving photosynthetic organisms regulate carbon metabolism through a light-dependent redox signalling pathway. Electrons are shuttled from photosystem I by means of ferredoxin (Fdx) to ferredoxin-thioredoxin reductase (FTR), which catalyses the two-electron-reduction of chloroplast thioredoxins (Trxs). These modify target enzyme activities by reduction, regulating carbon flow. FTR is unique in its use of a [4Fe-4S] cluster and a proximal disulphide bridge in the conversion of a light signal into a thiol signal. We determined the structures of FTR in both its one- and its two-electron-reduced intermediate states and of four complexes in the pathway, including the ternary Fdx-FTR-Trx complex. Here we show that, in the first complex (Fdx-FTR) of the pathway, the Fdx [2Fe-2S] cluster is positioned suitably for electron transfer to the FTR [4Fe-4S] centre. After the transfer of one electron, an intermediate is formed in which one sulphur atom of the FTR active site is free to attack a disulphide bridge in Trx and the other sulphur atom forms a fifth ligand for an iron atom in the FTR [4Fe-4S] centre--a unique structure in biology. Fdx then delivers a second electron that cleaves the FTR-Trx heterodisulphide bond, which occurs in the Fdx-FTR-Trx complex. In this structure, the redox centres of the three proteins are aligned to maximize the efficiency of electron transfer from the Fdx [2Fe-2S] cluster to the active-site disulphide of Trxs. These results provide a structural framework for understanding the mechanism of disulphide reduction by an iron-sulphur enzyme and describe previously unknown interaction networks for both Fdx and Trx (refs 4-6).     

Isolation and some properties of the heparin-neutralizing factor (PF4) released from human blood platelets

Zusammenfassung Der in Form eines hochmolekularen Komplexes von den Plättchen freigesetzte, heparinneutralisierende Faktor (PF 4) konnte reversibel in ein Träger-Material und ein aktives Protein (Molekulargewicht ca. 30000) aufgespalten werden.

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This work was supported by the Schweizerischer Nationalfonds zur Förderung der wissenschaftlichen Forschung.     

Effets inhibiteurs de l'acide tellurique sur le développement des tumeurs de Crown-gall chez la tomate

Summary Tellurium acid at 10^–3g/ml prevents every tumor formation, although allowing a normal development of the treated plants.