Publications by authors named "A P Wieslander"

Background/aims: Acid-base status is important for understanding pathophysiology, making a diagnosis, planning effective treatment and monitoring progress of critically ill patients. Manual calculations are cumbersome, easily result in wrong conclusions. We wanted to develop an automated assessment of acid-base status.

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Background/aims: Post-filter ionized calcium (iCa) measured on a blood gas analyzer (BGA) during regional citrate anticoagulated continuous renal replacement therapy (CRRT) are needed to control the regime. This increases the workload and requires attention including interpretation of blood analyses. Two algorithms were developed to calculate the post-filter iCa instead.

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Background: The aim of this study was to investigate in vitro biocompatibility of Reguneal™, a new bicarbonate containing peritoneal dialysis fluid (PDF) for Japan, and compare it with other PDFs available in that country.

Methods: We assessed basal cytotoxicity using in vitro proliferation of cultured fibroblasts, L-929, determining the quantity of living cells by the uptake of Neutral Red. Levels of ten glucose degradation products (GDPs) were measured by a validated ultrahigh-performance liquid chromatography method in combination with an ultraviolet detector.

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WaaG is a glycosyltransferase that is involved in the biosynthesis of lipopolysaccharide in Gram-negative bacteria. Inhibitors of WaaG are highly sought after as they could be used to inhibit the biosynthesis of the core region of lipopolysaccharide, which would improve the uptake of antibiotics. Herein, we establish an activity assay for WaaG using (14)C-labeled UDP-glucose and LPS purified from a ∆waaG strain of Escherichia coli.

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The Cpx stress response system is induced by various environmental and cellular stimuli. It is also activated in Escherichia coli strains lacking the major phospholipid, phosphatidylethanolamine (PE). However, it is not known whether CpxA directly senses changes in the lipid bilayer or the presence of misfolded proteins due to the lack of PE in their membranes.

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