Nanostructures originales obtenues par décomposition catalytique d'hydrocarbure

National audienceL'arc électrique et la décomposition catalytique d'hydrocarbures peuvent produire diverses nanostructures de carbone, telles que fullerènes, nanotubes, nanofibres et autres particules nanométriques de carbone. Une publication récente1 décrit la préparation et la séparation de nanobâtonnets de carbone dans la suie produite par arc électrique. Ici nous présentons la fabrication de nanobâtonnets de carbone par décomposition catalytique d'hydrocarbures, ainsi que des fibrilles de quelques nanomètres de diamètre et de quelques dizaines de nanomètres de longueur poussant perpendiculairement à la particule de catalyseur

Fabrication de carbure de titane par combustion auto-entretenue de titane et de carbone : initiation par diffusion à l'état solide

Self-propagating high temperature synthesis of titanium carbide from finely divided powders of Ti and C is initiated in the solid state by diffusion at the contacts between particles. In the model of concentric spheres of titanium and carbon, the formation of TiC has been computerized as a function of graphite particles radius r(m), time t(s) and absolute temperature T(K). The reaction rate α (moles of carbon reacted relative to the initial amount of carbon) can be expressed by the relationship : [MATH

Frog diazepam-binding inhibitor: peptide sequence, cDNA cloning, and expression in the brain.

Three peptides derived from diazepam-binding inhibitor (DBI) were isolated in pure form from the brain of the frog Rana ridibunda. The primary structures of these peptides showed that they correspond to mammalian DBI-(1-39), DBI-(58-87), and DBI-(70-87). A set of degenerate primers, whose design was based on the amino acid sequence data, was used to screen a frog brain cDNA library. The cloned cDNA encodes an 87-amino acid polypeptide, which exhibits 68% similarity with porcine and bovine DBI. Frog DBI contains two paired basic amino acids (Lys-Lys) at positions 14-15 and 62-63 and a single cysteine within the biologically active region of the molecule. Northern blot analysis showed that DBI mRNA is expressed at a high level in the brain but is virtually absent in peripheral tissues. The distribution of DBI mRNA and DBI-like immunoreactivity in the frog brain was studied by in situ hybridization and immunocytochemistry. Both approaches revealed that the DBI gene is expressed in ependymal cells and circumventricular organs lining the ventricular cavity. Since amphibia diverged from mammals at least 250 million years ago, the data show that evolutionary pressure has acted to conserve the structure of DBI in the vertebrate phylum. The distribution of both DBI mRNA and DBI-like immunoreactivity indicates that DBI is selectively expressed in glial cells

Occurrence of two somatostatin variants in the frog brain: characterization of the cDNAs, distribution of the mRNAs, and receptor-binding affinities of the peptides.

In tetrapods, only one gene encoding a somatostatin precursor has been identified so far. The present study reports the characterization of the cDNA clones that encode two distinct somatostatin precursors in the brain of the frog Rana ridibunda. The cDNAs were isolated by using degenerate oligonucleotides based on the sequence of the central region of somatostatin to screen a frog brain cDNA library. One of the cDNAs encodes a 115-amino acid protein (prepro-somatostatin-14; PSS1) that exhibits a high degree of structural similarity with the mammalian somatostatin precursor. The other cDNA encodes a 103-amino acid protein (prepro-[Pro2, Met13]somatostatin-14; PSS2) that contains the sequence of the somatostatin analog (peptide SS2) at its C terminus, but does not exhibit appreciable sequence similarity with PSS1 in the remaining region. In situ hybridization studies indicate differential expression of the PSS1 and PSS2 genes in the septum, the lateral part of the pallium, the amygdaloid complex, the posterior nuclei of the thalamus, the ventral hypothalamic nucleus, the torus semicircularis and the optic tectum. The somatostatin variant SS2 was significantly more potent (4-6 fold) than somatostatin itself in displacing [125I-Tyr0, D-Trp8] somatostatin-14 from its specific binding sites. The present study indicates that the two somatostatin variants could exert different functions in the frog brain and pituitary. These data also suggest that distinct genes encoding somatostatin variants may be expressed in the brain of other tetrapods

Proopiomelanocortin Gene Expression in the Ovary of the Frog, Rana esculentaa

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