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We report on the intrinsically limited low-field mobility of the two-dimensional electron gas (2DEG) in gated AlGaN/GaN and AlGaN/AlN/GaN heterostructures. Monte Carlo transport simulations are carried out to calculate the room-temperature 2DEG mobilities in dependence on the electron sheet density. The simulated 2DEG mobilities are compared to the phonon-limited mobility of bulk GaN. We estimate a maximum 2DEG mobility of about 2700 cm2 V-1 s-1 for an electron sheet density of ∼5×1012 cm-2, which remarkably exceeds the phonon-limited bulk mobility of 1520 cm2 V-1 s-1. By reducing the electron sheet density below 5×1012 cm-2, i.e., in a weak electron quantum confinement regime, the room-temperature 2DEG mobility gradually decreases and approaches the phonon-limited bulk value for vanishing quantum confinement. The insertion of a thin AlN barrier interlayer improves transport properties of the 2DEG and the mobility substantially increases due to a suppression of the alloy scattering. [ABSTRACT FROM AUTHOR]

Experiments based on neuronal cell-transistor couplings were made from some groups during the last years. Pioneering work in this field was carried out by Fromherz and his group (Fromherz, 2003; Schmidtner and Fromherz, 2006). We were interested of the interaction of nerve cells to serine hydrolase inhibitor diisopropylfluorophosphate (DFP), monitored by using an aluminum-galliumnitride/galliumnitride (AlGaN/GaN) electrolyte gate field effect transistor (EGFET). The biocompatibility study of our sensor materials with nerve cells shows a proliferation rate of at least 95%. The inhibitors were added to the medium and the source-drain current of the EGFET was recorded as a function of time. The inhibitor was added to the NG108-15 nerve cells growing directly on the sensor surface, resulting in a fast decrease in the drain current, I(DS). Control measurements show that this response is associated with cationic fluxes pumped through ionic channels present in the cellular membrane. The sensor enables analysis of the ion channel activity without cell destruction and simultaneously allows visual observation due to the optical transparency of the sensor material., (Copyright © 2012 Elsevier B.V. All rights reserved.)

The oldest account book ever found for the Bavarian monastery of Aldersbach records the existence of physicians in the Episcopal city of Würzburg in 1291-2. The anonymous Cistercian monk who recorded this account wrote in detail about a few academic physicians, phisici. But there are also some rather interesting occurrences recorded in the book. The abbot of Aldersbach at the time, Henry, suffered from a rather severe illness, and the book allows us to follow the path of this illness to some medical authorities at the end of the 13th century. He met physicians in Würzburg and Paris, which was the centre of the medical field in Central Europe at the time. Ultimately no-one was able to help Henry, and in his last try to get medical help he looked to the highest of all physicians in the medieval thinking; Christ himself. He made a pilgrimage to the lacrimae Christi, a relic probably presented in Regensburg, but died on the 26th of September 1295.

Monoclonal antibodies were isolated which reacted specifically with the complement cleavage products C3a, C3adR, C5a, and C5adR but not with the parent molecules C3 or C5. In both cases the mAbs showed a higher affinity towards the desArg forms. These mAbs were used as capture antibodies in immunoassays for C3a/C3adR and C5a/C5adR. The immunoassays are based on the ABICAP technology which ensures for a rapid measurement. Due to the large binding capacity and the very short diffusion pathways in the gel-matrix the binding equilibrium between capture antibodies and the antigen is reached whilst the sample is flowing through the column. Therefore this test represents an endpoint assay offering the possibility of using a single calibration curve for a large number of measurements. With the C3adR assay concentrations down to 16 ng/ml C3adR can be detected. The lower detection limit of the C5adR assay is 1 ng/ml C5adR. The tests for C3a/C3adR, and C5a/C5adR can be performed in 20 to 25 min and this rapid processing of plasma samples should permit the application of these parameters for diagnostic purposes and patient management.

Biological activities have been determined for a series of 18 peptides based on the C-terminal sequence of human or rat C5a. Lysosomal enzyme release was tested in two cell types, the promyelotic leukemia cell line U937 and polymorphonuclear leukocytes. In addition, an ATP-release assay with guinea pig platelets was performed. It was demonstrated that the C-terminal octapeptide 67-74 of human C5a represents the minimal sequence required to induce a measurable biological signal in all assays. Extending this peptide to a length of 21 amino acids produced at best only a slight enhancement of potency. Amino acid replacements with either tryptophanyl or phenylalanyl residues in positions between 65-69 either increased potency (at position 67), or abrogated potency (at position 66) in the two lysosomal enzyme assays. N-terminal acylation with the fluorenylmethoxy-carbonyl-aminohexanoyl group slightly enhanced C5a potency. In desensitization experiments with guinea pig platelets all peptides with a C5a activity were able to desensitize not only the C5a but also the C3a responses.