PubMed · 3869120
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H Kawahara. 1985. Materials for hard tissue replacement.. https://pubmed.ncbi.nlm.nih.gov/3869120/
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The technique which is described combines the advantages of the techniques formerly proposed in the literature in each stage of the preparation of transmission electron microscopy (TEM) specimens including a single metal-ceramic interface. It allows easy handling of the thin foils in spite of their brittleness. Preferential thinning of the softer material in the two-phase foil is prevented, and both sides of the interface are thinned down to comparable thicknesses. The nickel-alumina bicrystal interface observed in TEM is neat and free from any reaction layer. This method is easily adaptable to other metal-ceramic systems.
Automation of the clean-up procedure for trichothecenes on a charcoal-alumina column is described. Standard high-performance liquid chromatographic equipment was used for the clean-up step. An acetonitrile-water (84 + 16, v/v) extract of the sample was cleaned up on a column packed with charcoal-alumina-Celite, which was washed with acetonitrile between each sample. The eluates were collected directly in reaction vials and evaporated to dryness. The residual water was removed azeotropically with benzene. The sample was derivatized with 1-(trimethylsilyl)imidazole and analysed by capillary gas chromatography with electron-capture detection.
Interactions of an enzyme with an organized amphipilic bilayer are explored as a general means of enzyme immobilization in electroenzymatic systems. Immobilization of Desulfovibrio gigas hydrogenase at the electrode surface involves hydrophobic interactions of the enzyme with the bilayer assembly consisting of octadecyltrichlorosilane and octadecylviologen (C18MV2+) molecules. Due to a hydrophobic character of the enzyme, these interactions direct the enzyme to occupy a central position in the bilayer's hydrocarbon region and lead to immobilization of 3 pmol/cm2 of the enzyme in the plane of the bilayer. This corresponds to 50% surface coverage. The immobilized enzyme catalyzes H2 oxidation mediated by the C18MW2+/.+ couple. This electroenzymatic scheme functions under steady-state voltammetric as well as potentiometric conditions in the pH range 3.5-10. Coupling of enzymatic activity to the electrode surface is accomplished via lateral diffusion of the octadecylviologen molecules along the bilayer assembly.