Pre-Hemoglobin A, Glycosylated (PreHbA)

In vitro the rate of synthesis of the aldiminic linkage between Hb and glucose depends on glucose concentration, length of incubation and some other physiological factors. The content of HbA1 (stable glycosylated hemoglobin) is able to negatively affect the rate of synthesis of new pre-A1, according to a curvilinear model. These results suggest that in vitro the glycosylation process is saturable, and that elevated values of HbA1 are able to slow the synthesis of pre-A1 in vitro. The ion-exchange and affinity chromatography method proved to be independent of the amount of pre-HbA1c present. The electrophoresis method was independent of temperature in contrast to the other two methods, which showed a strong and comparable temperature dependency. Both ion-exchange and electrophoresis showed significant interference by changes in haemoglobin concentrations, whereas the protein concentration significantly biased the affinity chromatography figures.