Assessment of Gender Bias During Paramedic-Physician Handoffs.

Objective Gender bias against female physicians has been frequently demonstrated and associated with negative feelings toward their careers. Gender bias has also been demonstrated in prehospital clinical care. However, potential gender bias during paramedic-physician handoffs has not been studied. This study aimed to identify gender bias during interactions between prehospital personnel and emergency physicians at the time of patient handoff. Methods An observational study was conducted at an urban academic emergency department. Observers were trained to record information from paramedic-physician handoffs but were blind to the nature of the study. The primary outcome was to whom paramedics initially directed the focus of their handoff report based on physician gender, with secondary outcomes of to whom paramedics directed most of their report and whether they asked about further questions based on physician gender. Results There were 784 observed handoffs. There was no significant association between the gender of the physician and which physician received first attention (χ2 {1, N = 782} = 0.9736, p = 0.3238) or majority attention (χ2 {1, N = 780} = 1.9414, p = 0.1635). Paramedics were more likely to ask questions to male attendings than female attendings (χ2 {1, N = 784} = 4.4319, p = 0.0353). Conclusion We identified limited differences in communication based on gender between paramedics and physicians during emergency department patient handoffs.

Automated mass correction and data interpretation for protein open-access liquid chromatography-mass spectrometry.

Characterization of recombinant protein purification fractions and final products by liquid chromatography-mass spectrometry (LC/MS) are requested more frequently each year. A protein open-access (OA) LC/MS system was developed in our laboratory to meet this demand. This paper compares the system that we originally implemented in our facilities in 2003 to the one now in use, and discusses, in more detail, recent enhancements that have improved its robustness, reliability, and data reporting capabilities. The system utilizes instruments equipped with reversed-phase chromatography and an orthogonal accelerated time-of-flight mass spectrometer fitted with an electrospray source. Sample analysis requests are accomplished using a simple form on a web-enabled laboratory information management system (LIMS). This distributed form is accessible from any intranet-connected company desktop computer. Automated data acquisition and processing are performed using a combination of in-house (OA-Self Service, OA-Monitor, and OA-Analysis Engine) and vendor-supplied programs (AutoLynx, and OpenLynx) located on acquisition computers and off-line processing workstations. Analysis results are then reported via the same web-based LIMS. Also presented are solutions to problems not addressed on commercially available, small-molecule OA-LC/MS systems. These include automated transforming of mass-to-charge (m/z) spectra to mass spectra and automated data interpretation that considers minor variants to the protein sequence-such as common post-translational modifications (PTMs). Currently, our protein OA-LC/MS platform runs on five LC/MS instruments located in three separate GlaxoSmithKline R&D sites in the US and UK. To date, more than 8000 protein OA-LC/MS samples have been analyzed. With these user friendly and highly automated OA systems in place, mass spectrometry plays a key role in assessing the quality of recombinant proteins, either produced at our facilities or bought from external sources, without dedicating extensive amounts of analyst resource.

Protein open-access liquid chromatography/mass spectrometry.

Each year increasing numbers of proteins are submitted for routine characterization by liquid chromatography/mass spectrometry (LC/MS). This paper reports a solution that transforms routine LC/MS analysis of proteins into a fully automated process that significantly reduces analyst intervention. The solution developed, protein open-access (OA) LC/MS, consists of web-enabled sample submission and registration, automated data processing, data interpretation, and report generation. Sample submissions and results are recorded in a LIMS that utilizes an Oracle database. The protein sequence is captured during the sample submission process, stored in the database, and utilized to determine the theoretical protein molecular weight. This calculated mass is used to set the parameters for transformation of the mass-to-charge spectra to the mass domain and evaluate the presence or absence of the desired protein. Three protein OA-LC/MS instruments have been deployed in our facility to support protein characterization, purification, and modification efforts.