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C W Siebelder

Publications and source records attributed to C W Siebelder.

3 recordsLinked to original sources
PubMed1997

Capillary electrophoresis system for hemoglobin A1c determinations evaluated.

Hb A1c is the analyte of choice for monitoring metabolic control in patients with diabetes mellitus. Here we present a new analytical technique for measuring Hb A1c, capillary electrophoresis. The Hb A1c determination is not influenced by the labile Hb A1c fraction or by carbamylated or acetylated hemoglobin derivatives. Also, hemoglobin variants (Hb F, Hb S, and Hb C) do not interfere. This new application of capillary electrophoresis seems to be a valuable analytical tool for measuring Hb A1c in the clinical laboratory.

Blood Protein Electrophoresis↗
PubMed1993

Interference of carbamylated and acetylated hemoglobins in assays of glycohemoglobin by HPLC, electrophoresis, affinity chromatography, and enzyme immunoassay.

In vitro-synthesized carbamylated and acetylated hemoglobins interfered in assays of glycohemoglobin by HPLC and electrophoresis but had no effects on results obtained by affinity chromatography and enzyme immunoassay. Correlations between long-term serum urea concentrations and glycohemoglobin percentages revealed that, in vivo, carbamylated hemoglobin equivalent to 0.063% of total hemoglobin is formed for every 1 mmol/L of serum urea. The use of acetylsalicylate, either chronically in small doses (200-300 mg/day) or for 1 week at 2000 mg/day, did not cause significant interference from acetylhemoglobin, formed in vivo. We conclude that interference from carbamylated hemoglobin explains only a small part of existing discrepancies between results of glycohemoglobin assays in current use. The interfering effect of acetylhemoglobin formed in vivo with acetyl-CoA as substrate is as yet unknown.

Acetylation↗