This paper examines current interventions to reduce barriers to access into higher education for refugees in North America and Europe. We analyze a diversity of interventions sponsored by host governments, higher education institutions, foundations, nongovernmental organizations, and individuals. These interventions differ in size, delivery method, focus, and extent of support, and range from a single language course or limited online learning opportunity to fully accredited higher education programs. However, significant problems hamper the efficacy of many current interventions. We examine providers’ rationales for working with refugees using Knight and De Wit’s rationales for internationalization of higher education, later reconceptualized in four interrelated groups of rationales: academic, political, economic, and socio-cultural. To these, we propose adding a fifth category: humanism. To widen refugee participation and success in higher education, we suggest that policy makers and administrators should adopt a longer-term perspective, increase transparency, and use evidence-based approaches to develop and evaluate refugee programming.
Various separation modes in HPLC, such as anion exchange (AE), reversed-phase (RP), and affinity (AF) chromatography were examined for the separation of selenium species in human blood serum and urine. While RP-and AE-HPLC were mainly used for the separation of small molecular selenium species, double column AF-HPLC achieved the separation of selenoproteins in blood serum efficiently. Further, the effluent of AF-HPLC was enzymatically hydrolyzed and then analyzed with RP HPLC for selenoamino acid study. The versatility of the hybrid technique makes the in-depth study of selenium species possible. For quantification, post column isotope dilution (ID) with
78Se spike was performed. ORC ICP/MS (octapole reaction cell inductively coupled plasma/mass spectrometry) was used with 4 mL min −1 Hydrogen as reaction gas. In urine sample, inorganic selenium and SeCys were identified. In blood serum, selenoproteins GPx, SelP and SeAlb were detected and quantified. The concentration for GPx, SelP and SeAlb was 22.8 ± 3.4 ng g Enzymatic hydrolysis of each selenium proteins revealed that SeCys is the major amino acid for all three proteins and SeMet is contained in SeAlb only.
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