Quantum dots in Si/SiGe 2DEGs with Schottky top-gated leads

We report on the fabrication and characterization of quantum dot devices in a Schottky-gated silicon/silicon-germanium two-dimensional electron gas (2DEG). The dots are confined laterally inside an etch-defined channel, while their potential is modulated by an etch-defined 2DEG gate in the plane of the dot. For the first time in this material, Schottky top gates are used to define and tune the tunnel barriers of the dot. The leakage current from the gates is reduced by minimizing their active area. Further suppression of the leakage is achieved by increasing the etch depth of the channel. The top gates are used to put the dot into the Coulomb blockade regime, and conductance oscillations are observed as the voltage on the side gate is varied.Comment: New Fig. 1, submitted to New Journal of Physic

Identification of a major serum DNA-binding protein as factor B of the alternative complement pathway.

Abstract One of the major proteins in human serum capable of binding DNA has been shown to be factor B of the alternative pathway of complement activation. This protein, designated DNA-binding protein-2 (DBP-2), is recognized by antisera directed against both factor B and its activated form, fragment Bb. Its m.w., charge microheterogeneity, and amino acid composition correspond closely with reported values for those properties of factor B. A radioimmunoassay was used to estimate the serum concentration of DBP-2 at 266 +/- 83 microgram/ml, which also corresponds with the level of factor B normally present in the serum. DBP-2 functions as factor B in the activation of factor B-depleted serum. Limited proteolytic treatment of DBP-2 produced a fragment pattern resembling that of factor B both in the m.w. of the fragments and their electrophoretic mobilities. By means of DNA affinity chromatography of the fragments produced by trypsinization, the DNA-binding domain of DBP-2 was localized.</jats:p

Malar mass due to Actinomyces odontolyticus

Actinomyces odontolyticus was isolated from a patient with a soft tissue mass in the malar region. The organism was identified on the basis of morphological, cultural, and biochemical characteristics. On histological examination, the tissue mass contained several granulomatous foci with small, basophilic staining areas resembling microscopic sulfur granules. This is believed to be the first reported case of actinomycosis due to A. odontolyticus.</jats:p

Characterization of the autoantigen calreticulin.

Abstract Anti-Ro/SS-A antibodies are commonly found in the sera of patients with Sjögren's syndrome and SLE. These antibodies also occur in the mothers of children with neonatal lupus and congenital heart block. Ro/SS-A is a ribonucleoprotein complex whose cellular function remains unknown. To study its cellular function and to characterize its immunoreactivity, we have used an oligonucleotide designed after the published amino terminal sequence of a putative 60-kDa Ro/SS-A autoantigen to isolate its cDNA. This cDNA encodes a polypeptide that is the human homologue of calreticulin, a calcium binding protein of the endoplasmatic reticulum. The encoded polypeptide also shows a 64.4% identity with RAL-1, an Ag of the river blindness pathogen Onchocerca volvulus. Contrary to the data published by other authors, our results indicate that calreticulin is not a Ro/SS-A autoantigen. Moreover, we show that anticalreticulin autoantibodies occur in the sera of patients with SLE and patients with onchocerciasis.</jats:p