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Dedicated Software (dedicated + software)
Selected AbstractsFeasibility and usefulness of dedicated software and e-mail for self-monitoring blood glucose in treating diabetesDIABETIC MEDICINE, Issue 8 2002L. Perlemuter No abstract is available for this article. [source] Three-dimensional sonographic evaluation of gallbladder contractility: Comparison with cholescintigraphyJOURNAL OF CLINICAL ULTRASOUND, Issue 3 2006Hei Ja Yoon MD Abstract Purpose: To compare three-dimensional sonography (3D US) with quantitative cholescintigraphy for assessing gallbladder contractility. Methods: Gallbladder radioactivity was assessed in 35 patients with suspected gallbladder disease using a gamma camera 5, 30, 60, and 90 minutes after technetium 99m (Tc-99m) DISIDA injection and 30 and 60 minutes after ingestion of a high-fat meal. Immediate gallbladder images were obtained via 3D US. Gallbladder radioactivity at 120 minutes after injection of Tc-99m DISIDA was defined as 100%, and gallbladder contractility was calculated. Gallbladder volume on 3D US was calculated using a dedicated software. Pearson correlation analysis and simple linear regression analysis were used. Results: The mean gallbladder volume on 3D US was 25.3 ml after fasting and 6.6 ml after a high-fat meal. The mean gallbladder contractility index was 77.7% on cholescintigraphy (range, 18,99) and 73.4 on 3D US (range, 16.7,97.3). A linear correlation between cholescintigraphy and 3D US contractility indices was observed. The r value on Pearson analysis was 0.92 and R2 of the coefficient of determination was 0.85. The difference in measured contractility between the 2 methods ranged from +21.5% to ,15.0% (mean ± SD, 4.4 ± 8.7%). Conclusions: 3D US is a reliable and easy method for clinical measurement of the volume of the gallbladder and its contractility. © 2006 Wiley Periodicals, Inc. J Clin Ultrasound 34:123,127, 2006 [source] Chemical cross-linking with NHS esters: a systematic study on amino acid reactivitiesJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 5 2009Stefanie Mädler Abstract Structure elucidation of tertiary or quaternary protein structures by chemical cross-linking and mass spectrometry (MS) has recently gained importance. To locate the cross-linker modification, dedicated software is applied to analyze the mass or tandem mass spectra (MS/MS). Such software requires information on target amino acids to limit the data analysis time. The most commonly used homobifunctional N-hydroxy succinimide (NHS) esters are often described as reactive exclusively towards primary amines, although side reactions with tyrosine and serine have been reported. Our goal was to systematically study the reactivity of NHS esters and derive some general rules for their attack of nucleophilic amino acid side chains in peptides. We therefore studied the cross-linking reactions of synthesized and commercial model peptides with disuccinimidyl suberate (DSS). The first reaction site in all cases was expectedly the ,-NH2 -group of the N -terminus or the ,-NH2 -group of lysine. As soon as additional cross-linkers were attached or loops were formed, other amino acids were also involved in the reaction. In addition to the primary amino groups, serine, threonine and tyrosine showed significant reactivity due to the effect of neighboring amino acids by intermediate or permanent Type-1 cross-link formation. The reactivity is highly dependent on the pH and on adjacent amino acids. Copyright © 2009 John Wiley & Sons, Ltd. [source] Rapid analysis of food products by means of high speed gas chromatographyJOURNAL OF SEPARATION SCIENCE, JSS, Issue 4 2007Paola Donato Abstract Since the invention of GC, there has been an ever increasing interest within the chromatographic community for faster GC methods. This is obviously related to the fact that the number of samples subjected to GC analysis has risen greatly. Nowadays, in routine analytical applications, sample throughput is often the most important aspect considered when choosing an analytical method. Gas chromatographic instrumentation, especially in the last decade, has been subjected to continuous and considerable improvement. High-speed injection systems, electronic gas pressure control, rapid oven heating/cooling and fast detection are currently available in a variety of commercial gas chromatographs. The main consequence of this favourable aspect is that high-speed GC is being increasingly employed for routine analysis in different fields. Furthermore, the employment of dedicated software makes the passage from a conventional to a fast GC method a rather simple step. The present review provides an overview of the employment of fast GC techniques for the analysis of food constituents and contaminants. A brief historical and theoretical background is also provided for the approaches described. [source] Comparative LC-MS: A landscape of peaks and valleysPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 4 2008Antoine H. P. America Dr. Abstract Quantitative proteomics approaches using stable isotopes are well-known and used in many labs nowadays. More recently, high resolution quantitative approaches are reported that rely on LC-MS quantitation of peptide concentrations by comparing peak intensities between multiple runs obtained by continuous detection in MS mode. Characteristic of these comparative LC-MS procedures is that they do not rely on the use of stable isotopes; therefore the procedure is often referred to as label-free LC-MS. In order to compare at comprehensive scale peak intensity data in multiple LC-MS datasets, dedicated software is required for detection, matching and alignment of peaks. The high accuracy in quantitative determination of peptide abundancies provides an impressive level of detail. This approach also requires an experimental set-up where quantitative aspects of protein extraction and reproducible separation conditions need to be well controlled. In this paper we will provide insight in the critical parameters that affect the quality of the results and list an overview of the most recent software packages that are available for this procedure. [source] | |||||||||||||