Objectives: The stability of the analytes most commonly used in routine clinical practice has been the subject of intensive research, with varying and even conflicting results. Such is the case of alanine aminotransferase (ALT). The purpose of this study was to determine the stability of serum ALT according to different variables.
Methods: A multicentric study was conducted in eight laboratories using serum samples with known initial catalytic concentrations of ALT within four different ranges, namely: <50 U/L (<0.83 μkat/L), 50-200 U/L (0.83-3.33 μkat/L), 200-400 U/L (3.33-6.67 μkat/L) and >400 U/L (>6.67 μkat/L). Samples were stored for seven days at two different temperatures using four experimental models and four laboratory analytical platforms. The respective stability equations were calculated by linear regression. A multivariate model was used to assess the influence of different variables.
Results: Catalytic concentrations of ALT decreased gradually over time. Temperature (-4%/day at room temperature vs. -1%/day under refrigeration) and the analytical platform had a significant impact, with Architect (Abbott) showing the greatest instability. Initial catalytic concentrations of ALT only had a slight impact on stability, whereas the experimental model had no impact at all.
Conclusions: The constant decrease in serum ALT is reduced when refrigerated. Scarcely studied variables were found to have a significant impact on ALT stability. This observation, added to a considerable inter-individual variability, makes larger studies necessary for the definition of stability equations.
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http://dx.doi.org/10.1515/almed-2020-0021 | DOI Listing |
Mikrochim Acta
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Cellular and Molecular Research Center, Cellular and Molecular Research Medicine Institute, Urmia University of Medical Sciences, 5714783734, Urmia, Iran.
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Research Focus Area for Chemical Resource Beneficiation, Catalysis and Synthesis Research Group, North-West University, 11 Hoffman Street, Potchefstroom 2522, South Africa.
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View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Department of Earth Resources and Environmental Engineering, Hanyang University, Seoul 04763, Republic of Korea. Electronic address:
Kraft lignin (KL), a byproduct of the pulp and paper industry, is commonly combusted as a low-grade fuel. However, its high sulphur content results in the emission of sulphur oxides, which pose environmental hazards. This study explores a sustainable approach for the valorisation of waste KL into syngas via CO-mediated pyrolysis.
View Article and Find Full Text PDFJ Am Chem Soc
January 2025
Department of Chemistry, University of California, Berkeley, California 94720, United States.
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View Article and Find Full Text PDFInsulin degrading enzyme (IDE) is a dimeric 110 kDa M16A zinc metalloprotease that degrades amyloidogenic peptides diverse in shape and sequence, including insulin, amylin, and amyloid-β, to prevent toxic amyloid fibril formation. IDE has a hollow catalytic chamber formed by four homologous subdomains organized into two ∼55 kDa N- and C-domains (IDE-N and IDE-C, respectively), in which peptides bind, unfold, and are repositioned for proteolysis. IDE is known to transition between a closed state, poised for catalysis, and an open state, able to release cleavage products and bind new substrate.
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