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Objectives: Pharmaceutical manufacturers recommend refrigerating succinylcholine at a temperature range of 2–8°C. With widespread use of prehospital succinylcholine on ambulances without refrigeration, it is important to understand the stability of this drug. Using mass spectrometry, this study investigated the degradation of the succinylcholine compound before and after its exposure to ambulance cabin temperatures, while removing light exposure. A 10% degradation threshold was set as not appropriate for human use, in accordance with U.S. Food and Drug Administration guidelines. Methods: The study used 17 vials of succinylcholine sealed with duct tape in light-resistant bags. The bags were placed in climate controlled compartments in two ambulances: one stationed in a garage and the other stationed outdoors. Mass spectrometry analysis was used to examine drug degradation at Time 0, the 14th day of the first month, and monthly from Time 0 to 7 months. Results: The degradation products of succinyl monocholine (SMC) and choline are already present at Day 0. Ten percent degradation was achieved at approximately 90 days into the experiment. Temperature in the ambulance climate controlled compartment was 70°F, with a range from 56 to 89°F during the 6-month time period. Conclusions: Identifiable breakdown fragments of succinylcholine have been identified using mass spectrometry with fresh drug upon receipt from the manufacturer. Ten percent degradation was not observed until approximately 90 days after being placed on ambulances. Temperature variations did not significantly contribute to degradation of succinylcholine, and it is safe for injection until approximately 90 days in similar climates. ACADEMIC EMERGENCY MEDICINE 2010; 17:631–637 © 2010 by the Society for Academic Emergency Medicine [ABSTRACT FROM AUTHOR]

Much of the difficulty associated with identifying and repatriating deceased undocumented border-crossers stems from an inability to narrow down the search area to more probable options. Analysis of the isotopic variation in the tooth enamel of modern Mexican populations is currently underway at the University of California Santa Cruz. Using Thermo Ionization Mass Spectrometry, the pilot research analyzed strontium isotopes located in the donated permanent teeth of Mexican-born individuals of known origin from four states. The preliminary results reveal the formation of three distinctly significant regions in the data set. Using the technology outlined here, a map documenting the isotopic variation in modern Mexican tooth enamel is being complied to use for cross comparison with deceased border crossers of unknown origin. [ABSTRACT FROM AUTHOR]

The article presents a critical review on the significant developments in the inductively coupled plasma mass spectrometry (ICPMS) in chemical research from October 2003 to October 2005 in the U.S. Due to the publication of numerous papers that do not represent a significant advancement in ICPMS, the author recommends rejection of some manuscripts. It is the goal of the refereeing process to ensure the quality and significance of published papers in the field. In conclusion, the marginal importance of many published papers indicate a large variation in the reviewing process within a given journal. Proper selection of referees is also considered in this review.

The article examines several developments in environmental mass spectrometry over the period of 2004 to 2005 in the U.S. Since the "Analytical Chemistry" periodical's policy limits reviews to include 100 to 200 significant references and to mainly focus on new trends, this paper will be limited in its focus to new, emerging contaminants and environmental issues of the most current research. Analytical methods include an increasing use of time-of-flight mass spectrometry and quadropole for structural elucidation and compound confirmation.

Abstract: High-field asymmetric waveform ion mobility spectrometry (FAIMS) is a new technology for ion separation at atmospheric pressure. This review introduces the reader to FAIMS, covering topics ranging from the fundamentals and extraction of physical parameters from the raw data, to applications of FAIMS extending from homeland security to environmental analysis to proteomics. The investigation of FAIMS as an ion pre-processing tool for mass spectrometry is in its infancy, but reports in the literature illustrate that FAIMS separates isobaric ions including diastereoisomers, separates isotopes, reduces background ions by isolating ions of interest, and simplifies spectra of complex mixtures by dividing the mixture into a series of simpler subsets of ions. Applications ranging from quantitative analysis of inorganic and organometallic compounds, to studies of the conformers of intact proteins, have been reported. This review is a launching point for further exploration of FAIMS. [Copyright &y& Elsevier]

The article discusses the significance of mass spectrometry (MS) technology in the U.S. The MS was started by Carlos Lebrilla at the University of California. This technology was initially used only by physical chemists to determine molecular structures, nuclear magnetic resonance (NMR). Mass spectrometry is a sensitive method for identifying individual molecules in complex mixtures, and could revolutionize everything from clinical testing to crime scene investigation. However, the technique has been considered too expensive and too difficult for deployment of specialized spectroscopy laboratories, so manufacturers have developed techniques that brings such problems away.

Information about the annual American Society of Mass Spectrometry meeting held in Minneapolis, Minnesota on June 9 to 13, 2013 is presented. Topics include the embryonic playground of editorial creativity. The meeting featured several representatives of the Associate Editorial Board including David Kilgour of Great Britain, Adam Trevitt of Australia and Sarah Trimpin of the U.S.

The article presents a spectroscopic study of charged biological molecules of cold, protonated tryptophan and tyrosine in their gas phases by electrospray in the U.S. Basing from the fluorescence lifetime of neutral tryptophan is on the order of nanoseconds, the results emphasizes the extreme sensitivity of the excited state dynamics to the influence of charge in its local environment.

The article reports on the effectiveness of cavity ring-down spectroscopy in carrying out isotope analysis in the U.S. It reveals that the process, developed by chemists at Stanfod University, has utilized cavity ring-down spectrometer which enable researchers to effectively evaluate isotope ratios, compared to isotope rate mass spectrometry (IRMS). Also, the instrument is inexpensive and has enhanced absorption rate.

Cadmium telluride (CdTe) thin film photovoltaic devices fabricated in a-line process developed at Colorado State University (CSU) have shown stability during long-term (over a 5 year period) accelerated stress testing. These devices have a copper (Cu) containing back contact. The Cu profile as measured by secondary ion mass spectrometry characterization shows, for the maximum stressed device (23,399 h), that there is a significant (two times) change in the concentration of secondary Cu ions in the bulk of the material; however, the Cu concentration gradient at the back of the device has no significant change, and the CdS layer has no significant Cu concentration increase at open-circuit bias and 65°C temperature conditions. This indicates that with a proper CdCl2 treatment, Cu can be used to form the back contact for CdTe devices with acceptable stability. These devices have a projected field lifetime of greater than 60 years. [ABSTRACT FROM AUTHOR]

The article reports that the U.S. National Aeronautics and Space Administration's (NASA) Phoenix mission has landed in Mars on May 26, 2008. It has landed about 30 kilometers from its intended set-down point in the planet's northern plains. The arrival of the mission marks the first successful soft landing on Mars by means of retrorockets. Meanwhile, the mission scientists will spend several days checking and calibrating instruments before collecting samples for mass spectrometry and chemical analysis of the planet.

The article focuses on the functionality of proteins from tissue samples that have been formalin-fized and paraffin-embedded (FFPE) by Expression Pathology in the U.S. The Pathology was founded in 2001 which was considered as pioneering in Tissue Microproteomics for isolating and extracting proteins from FFPE tissue samples for analysis by mass spectrometry or reverse-phase dot blot arrays. The company has developed a technology that integrates extraction of total proteins from FFPE samples with cryptic digestion. Other companies that provide tissue isolation include QIAGEN and EMD Chemicals which offer systems chemically reverse formalin crosslinking and post-transnational modifications (PTMs) for phosphorylation and acetylation of proteins.

The article reports on the addition of Waters Synapt High Definition Mass Spectrometry (HDMS) system to Max Plank Institute in the U.S. The system aims to enhance the Institute's research on neurodegenerative diseases. It was delivered by its Department of Cellular Biochemistry to study proteins in causing brain-wasting diseases. It will be used in analyzing the large protein complexes and their subunit composition.

The article reports that Steven Boxer and colleagues at Stanford University, Lawrence Livermore National Laboratory, and the University of California, have demonstrated the ability to produce quantitative maps of lipid composition in artificial bilayers at resolution of ~100 nanometer by combining atomic force microscopy with secondary ion mass spectroscopy. The researchers used a method to pattern intact fluid lipid bilayers on a silicon wafer and prepared the supported lipid membranes from vesicles containing equal mole fractions of N-labeled 1,2-dilauroylphoshatidylcholine and C-labeled 1,2-distearoylphosphatidylcholine.

This article reports that the Academy Savant's CD-based program, "Introduction to Peptide and Protein Analysis with Mass Spectrometry" includes molecular weight determinations, mass mapping, and sequencing with MS-MS with easy-to-follow animations. The more advanced techniques that allow analysts to study post-translational modifications of proteins, non-covalent interactions, and differences in protein expression in living tissues, are also presented. The program, which is based of the popular American Chemical Society course, begins with a description of basic protein chemistry for scientists who are new to the field.

The article presents a summary of the plenary lecture "Tandem Mass Spectrometry of Large Biomolecules," delivered by Fred W. McLafferty in the U.S. Key issues discussed include the best-recognized capabilities of mass spectrometry, the important applications of mass spectrometry in the structural characterization of large biomolecules from molecular dissociation, the value of tandem mass spectrometry for mixtures and a description of the features and benefits from using the Fourier-transform mass spectrometer.