Interference with the enzymic measurement of cholesterol in serum by use of five reagent kits.

  title={Interference with the enzymic measurement of cholesterol in serum by use of five reagent kits.},
  author={Michael A. Pesce and Selma H. Bodourian},
  journal={Clinical chemistry},
  volume={23 4},
We describe the effects of uric acid, hemolysis, drugs, ascorbic acid, lipemia, and bilirubin on the enzymic measurement of cholesterol in serum by use of reagent kits from Abbott, Beckman, Boehringer Mannheim, Calbiochem, and Worthington. In all of these, the chromogen formed from the reaction of hydrogen peroxide with phenol and 4-aminoantipyrene is measured. The absorbance was measured at 500 nm vs. a serum blank for each kit--except Abbott's with which the recorded absorbances were the… 
Enzymic serum cholesterol measurement with a basic autoanalyzer and Du Pont aca method.
Apparent cholesterol as measured with the aca became proportionately greater than AutoAnalyzer values with increasing serum triglyceride concentration.
Enzymic Assay of Plasma Cholesterol: A Comparison of Analytical Variations Found Using the Greiner GSA II and the Technicon SMA 12/60 and SMA II
  • J. Steinmetz, E. Panek, E. Gaspart
  • Chemistry, Medicine
    Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie
  • 1979
Cholesterol was assayed on the Greiner GSA II and the Technicon SMA 12/60 and SMA II autoanalyzers, with Allain's entirely enzymic method, and the results were in good agreement with those obtained by Abell's method.
Ascorbic acid interference in the measurement of serum biochemical parameters: in vivo and in vitro studies.
Serum levels of ascorbic acid increased significantly after vitamin C ingestion inhibiting urate and total bilirubin tests 4 and 12 h after intake, and commonly taken doses of supplementary vitamin C interfered negatively with the serum urate test based on the Trinder method, and with bilirube metabolism.
Cholesterol oxidase: thermochemical studies and the influence of hydroorganic solvents on enzyme activity.
Thermal and binary cosolvent studies of the cholesterol oxidase (cholesterol: oxygen oxidoreductase, EC 1.3.6) reaction have been carried out using batch microcalorimetry and ultraviolet spectrophotometry yielding results comparable to conventional automated clinical assay.
Determination of Total Cholesterol in Hypertriglyceridemic Serums
Abstract The determination of serum total cholesterol by a direct reaction involving a Trinder-type enzymic pathway can be severely hampered by the turbidity caused by excessive concentrations of
Vitamin C and aberrant electrolyte results
A 61-year-old lady with severe electrolyte abnormalities after administration of high doses of vitamin C is described, who had terminal colon cancer and presented to hospital with anuria.
Ecuaciones para Eliminar la Interferenciade Sueros Hemolisados, Ictéricose Hiperglucémicos en las DeterminacionesRutinarias de Química Clínica
Background: Specimens hyperglycemic, icteric or with hemolysis can produce interference at time of analysis, because the methods used in clinical chemistry determinations are based on
Serum-constituents analyses: effect of duration and temperature of storage of clotted blood.
Results obtained showed that total protein and calcium after 48 h at 30 degrees C and total cholesterol, triglycerides, beta-lipoprotein, serum urea nitrogen, creatinine, uric acid, and gamma-glutamyltransferase (EC were not influenced by storage at 4, 24, or30 degrees C for as long as 48 h.
Advantages and disadvantages of serum cholesterol determination by the kinetic vs the end point method.
The end point imprecision fell within National Cholesterol Education Program guidelines (<or=3%), but the kinetic did not and required shorter analysis time.
A coupled NAD+-peroxidase spectrophotometric assay for cholesterol.
A modified enzymic reagent for determination of cholesterol and cholesterol ester in serum and in high-density lipoprotein is described, using hydrogen peroxide produced by the action of cholesterol oxidase as a substrate for NAD+ peroxidase.