Development of hormone-responsive cell strains in vitro.
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Biomedical subjects
Publications and source records attributed to C A Hirsch.
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A soluble l-alpha-glycerophosphate dehydrogenase, which is stimulated by FAD and is independent of added pyridine nucleotides, functions during anaerobic catabolism of glycerol and l-alpha-glycerophosphate by Escherichia coli.
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Cyclosporine blood concentrations were simultaneously determined by radioimmunoassay (RIA) and high-performance liquid chromatography (HPLC) at multiple points in time in two patients receiving cyclosporine for immunosuppression following liver transplantation. Radioimmunoassay levels always exceed those determined by HPLC; however, the divergence between the two methods increased as serum bilirubin concentration increased, with HPLC:RIA ratios generally less than 0.3 when serum bilirubin concentrations exceeded 10.0 mg/dL. These preliminary results suggest that retention of immunoactive cyclosporine metabolites due to imparied liver function may account for RIA-determined cyclosporine concentrations that greatly exceed those measured by HPLC.