370 research outputs found

    Impact of thermal energy storage properties on solar dynamic space power conversion system mass

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    A 16 parameter solar concentrator/heat receiver mass model is used in conjunction with Stirling and Brayton Power Conversion System (PCS) performance and mass computer codes to determine the effect of thermal energy storage (TES) material property changes on overall PCS mass as a function of steady state electrical power output. Included in the PCS mass model are component masses as a function of thermal power for: concentrator, heat receiver, heat exchangers (source unless integral with heat receiver, heat sink, regenerator), heat engine units with optional parallel redundancy, power conditioning and control (PC and C), PC and C radiator, main radiator, and structure. Critical TES properties are: melting temperature, heat of fusion, density of the liquid phase, and the ratio of solid-to-liquid density. Preliminary results indicate that even though overalll system efficiency increases with TES melting temperature up to 1400 K for concentrator surface accuracies of 1 mrad or better, reductions in the overall system mass beyond that achievable with lithium fluoride (LiF) can be accomplished only if the heat of fusion is at least 800 kJ/kg and the liquid density is comparable to that of LiF (1880 kg/cu m

    Positron emission tomographic imaging of Copper 64- and Gallium 68-labeled chelator conjugates of the somatostatin agonist Tyr3-octreotate

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    The bifunctional chelator and radiometal have been shown to have a direct effect on the pharmacokinetics of somatostatin receptor (SSTR)-targeted imaging agents. We evaluated three Y3-TATE analogues conjugated to NOTA-based chelators for radiolabeling with 64 Cu and 68 Ga for small-animal positron emission tomographic/computed tomograhic (PET/CT) imaging. Two commercially available NOTA analogues, p-SCN-Bn-NOTA and NODAGA, were evaluated. The p-SCN-Bn-NOTA analogues were conjugated to Y3- TATE through β-Ala and PEG 8 linkages. The NODAGA chelator was directly conjugated to Y3-TATE. The analogues labeled with 64 Cu or 68 Ga were analyzed in vitro for binding affinity and internalization and in vivo by PET/CT imaging, biodistribution, and Cerenkov imaging ( 68 Ga analogues). We evaluated the effects of the radiometals, chelators, and linkers on the performance of the SSTR subtype 2–targeted imaging agents and also compared them to a previously reported agent, 64 Cu-CB-TE2A-Y3-TATE. We found that the method of conjugation, particularly the length of the linkage between the chelator and the peptide, significantly impacted tumor and nontarget tissue uptake and clearance. Among the 64 Cu- and 68 Ga-labeled NOTA analogues, NODAGA-Y3-TATE had the most optimal in vivo behavior and was comparable to 64 Cu-CB-TE2A-Y3-TATE. An advantage of NODAGA-Y3-TATE is that it allows labeling with 64 Cu and 68 Ga, providing a versatile PET probe for imaging SSTr subtype 2-positive tumors

    Collection and processing of shipboard ADCP velocities from the Barents Sea Polar Front Experiment

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    The Barents Sea Polar Front Experiment was a combined physical oceanography and acoustic tomography field study which took place from 6-26 August 1992. Both shipboard and moored data were collected in a 80 x 70 km experimental region on the south flank of Sptisbergen Bank about 60 km east of Bear Island. Of principal interest in this report are the data from an Acoustic Doppler Current Profier (ADCP) which was operated continuously during the experimental period as a part of the shipboard instrumentation aboard the USNS Barlett. The data from eight current meters deployed on three moorings in the experimental region are used to supplement the ADCP analysis. Preliminary results showed that velocities in the experimental region were dominated by semi-diurnal tides. The strong tidal oscilations dictated the use of a tide removal scheme to extract a steady flow component from the space-time grid of ADCP velocities. This report describes the configuration and operation of the ADCP, the space-time sampling grid on which the data were collected, the determination of absolute velocity from the ADCP measurements, and the application and results of a tide removal technique which allowed estimation of the sub-tidal flow.Funding was provided by the Office of Naval Research under Grant No. NOOOI4-90-J-1359

    Characterization of Glycated Proteins by \u3csup\u3e13\u3c/sup\u3eC NMR Spectroscopy

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    13C NMR spectroscopy has been used to characterize Amadori (ketoamine) adducts formed by reaction of [2-13C]glucose with free amino groups of protein. The spectra of glycated proteins were acquired in phosphate buffer at pH 7.4 and were interpreted by reference to the spectra of model compounds, N alpha-formyl-N epsilon-fructose-lysine and glycated poly-L-lysine (GlcPLL). The anomeric carbon region of the spectrum (approximately 90-105 ppm) of glycated cytochrome c was superimposable on that of N alpha-formyl-N epsilon-fructose-lysine, and contained three peaks characteristic of the alpha- and beta-furanose and beta-pyranose anomers of Amadori adducts to peripheral lysine residues on protein (pK alpha approximately 10.5). The spectrum of GlcPLL yielded six anomeric carbon resonances; the second set of three was displaced about 2 ppm to lower shielding of the first and was assigned to the Amadori adduct at the alpha-amino terminus (pK alpha approximately 7.5). The spectrum of glycated RNase was similar to that of GlcPLL, but contained a third set of three signals attributable to modification of active site lysine 41 (pK alpha approximately 8.8). The assignments for RNase were confirmed by analysis of spectra taken at pH 4 and under denaturing conditions. The spectrum of glycated hemoglobin was comparable to that of GlcPLL, and distinct resonances could be assigned to Amadori adducts at amino-terminal valine and intrachain N epsilon-lysine residues. Chemical analyses were performed to measure the relative extent of alpha- and epsilon-amino group modification in the glycated macromolecules, and the results were compared with estimates based on integration of the NMR spectra

    Estradiol and Follicleâ Stimulating Hormone as Predictors of Onset of Menopause Transitionâ Related Bone Loss in Preâ and Perimenopausal Women

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    The menopause transition (MT) may be an opportunity for early intervention to prevent rapid bone loss. To intervene early, we need to be able to prospectively identify preâ and perimenopausal women who are beginning to lose bone. This study examined whether estradiol (E2), or follicleâ stimulating hormone (FSH), measured in preâ and perimenopausal women, can predict significant bone loss by the next year. Bone loss was considered significant if bone mineral density (BMD) decline at the lumbar spine (LS) or femoral neck (FN) from a preâ or early perimenopausal baseline to 1â year after the E2 or FSH measurement was greater than the least detectable change. We used data from 1559 participants in the Study of Women’s Health Across the Nation and tested E2 and FSH as separate predictors using repeated measures modified Poisson regression. Adjusted for MT stage, age, race/ethnicity, and body mass index, women with lower E2 (and higher FSH) were more likely to lose BMD: At the LS, each halving of E2 and each doubling of FSH were associated with 10% and 39% greater risk of significant bone loss, respectively (pâ <â 0.0001 for each). At the FN, each halving of E2 and each doubling of FSH were associated with 12% (p = 0.01) and 27% (pâ <â 0.001) greater risk of significant bone loss. FSH was more informative than E2 (assessed by the area under the receiverâ operator curve) at identifying women who were more versus less likely to begin losing bone, especially at the LS. Prediction was better when hormones were measured in preâ or early perimenopause than in late perimenopause. Tracking withinâ individual change in either hormone did not predict onset of bone loss better than a single measure. We conclude that measuring FSH in the MT can help prospectively identify women with imminent or ongoing bone loss at the LS. © 2019 American Society for Bone and Mineral Research.Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/153118/1/jbmr3856_am.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/153118/2/jbmr3856.pd

    \u3csup\u3e13\u3c/sup\u3eC NMR Investigation of Nonenzymatic Glucosylation of Protein

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    Nonenzymatic glucosylation of protein is initiated by the reversible condensation of glucose in its open chain form with the amino groups on the protein. The initial product is an aldimine (Schiff base) which cyclizes to the glycosylamine derivative. The aldimine can undergo a slow Amadori rearrangement to yield the relatively stable ketoamine adduct which is structurally analogous to fructose. 13C NMR has been used to characterize these early products of nonenzymatic glucosylation, using RNase A as a model protein. C-1 of the beta-pyranose anomer of the glycosylamine was identified at 88.8 ppm in the spectrum of RNase glucosylated approximately 1:1 with D-[1-13C]glucose. C-1 of the Amadori product was also apparent in this spectrum, resonating as a pair of intense peaks at 52.7 and 53.1 ppm. The anomeric (C-2) resonances of the Amadori adduct were seen in the spectrum of RNase glucosylated approximately 1:1 with [U-13C]glucose. This spectrum was interpreted by comparison to the spectra of reference compounds: D-fructose, fructose-glycine, N alpha-formyl-N epsilon-fructose-lysine, and glucosylated poly-L-lysine. In the protein spectrum, the most intense of the C-2 resonances was that of the beta-fructopyranose anomer at 95.8 ppm. The alpha- and beta-fructofuranose anomers were also observed at 101.7 and 99.2 ppm, respectively. One unidentified signal in the anomeric region was observed in the spectra of poly-L-lysine and RNase, both glucosylated with [U-13C]glucose; no comparable resonances were observed in the spectra of the model compounds

    Androgen receptor mutations

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    Male sexual differentiation and development proceed under direct control of androgens. Androgen action is mediated by the intracellular androgen receptor, which belongs to the superfamily of ligand-dependent transcription factors. At least three pathological situations are associated with abnormal androgen receptor structure and function: androgen insensitivity syndrome (AIS), spinal and bulbar muscular atrophy (SBMA) and prostate cancer. In the X-linked androgen insensitivity syndrome, defects in the androgen receptor gene have prevented the normal development of both internal and external male structures in 46,XY individuals. Complete or gross deletions of the androgen receptor gene have not been found frequently in persons with complete androgen insensitivity syndrome. Point mutations at several different sites in exons 2–8 encoding the DNA- and androgen-binding domain, have been reported for partial and complete forms of androgen insensitivity. A relatively high number of mutations were reported in two different clusters in exon 5 and in exon 7. The number of mutations in exon 1 is extremely low and no mutations have been reported in the hinge region, located between the DNA-binding domain and the ligand-binding domain and which is encoded by the first half of exon 4. Androgen receptor gene mutations in prostate cancer are very rare and are reported only in exons 4–8. The X-linked spinal and bulbar muscle atrophy (SBMA; Kennedy's disease) is associated with an expanded length (> 40 residues) of one of the polyglutamine stretches in the N-terminal domain of the androgen receptor

    The androgen receptor: Functional structure and expression in transplanted human prostate tumors and prostate tumor cell lines

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    Abstract The growth of the majority of prostate tumors is androgen-dependent, for which the presence of a functional androgen receptor is a prerequisite. Tumor growth can be inhibited by blockade of androgen receptor action. However, this inhibition is transient. To study the role of the androgen receptor in androgen-dependent and androgen-independent prostate tumor cell growth, androgen receptor mRNA expression was monitored in six different human prostate tumor cell lines and tumors, which were grown either in vitro or by transplantation on (male) nude mice. Androgen receptor mRNA was clearly detectable in three androgen-dependent (sensitive) tumors and absent or low in three androgen-independent tumors. Growth of the LNCaP prostate tumor cell line can be stimulated both by androgens and by fetal calf serum. In the former situation androgen receptor mRNA expression is downregulated, whereas in the latter no effect on androgen receptor mRNA levels can be demonstrated. Sequence analysis showed that the androgen receptor gene from LNCaP cells contains a point mutation in the region encoding the steroid-binding domain, which confers an ACT coVon encoding a threonine residue to GCT, encoding alanine
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