Effects of Bovine Hemoglobin on Chemistry Testing: Pseudohemolysis or Real?
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Glycosylated hemoglobin was measured in Mystromys albicaudatus, a rodent model of diabetes mellitus, using a newly developed colorimetric assay. The mean glycosylated hemoglobin for non-diabetic Mystromys (n = 321) was 14.8 nmol hydroxymethylfurfural / 10 mg hemoglobin which is similar to that obtained in non-diabetic humans. Animals with a glycosylated hemoglobin value greater than 19 nmol hydroxymethylfurfural / 10 mg hemoglobin were characterized as diabetics. Significant correlations were found between glycosylated hemoglobin and both plasma glucose and urine glucose levels.
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The dependence of net charge and oxygen affinity of human hemoglobin upon hemoglobin concentration was reinvestigated. In contrast to earlier reports from various laboratories, both functional properties of hemoglobin were found to be independent of hemoglobin concentration. Two findings indicate a concentration-independent net charge of carbonmonoxy hemoglobin at pH 6.6: (A) The pH value of a given carbonmonoty hemoglobin solution remains constant at 6.6 when the hemoglobin concentration is raised from 10 to 40 g/dl, indicating that there is no change in protonation of titratable groups of hemoglobin: (b) the net charge of carbonmonoxy hemoglobin as estimated from the Donnan distribution of 22Na+ shows no dependence on hemoglobin concentration in this concentration range. The oxygen affinity of human hemoglobin was determined from measurements of oxygen concentrations in equilibrated samples using a Lex-O2-Con apparatus (Lexington Instruments, Waltham, Mass.). P50 averaged 11.4 mm Hg at 37 degrees C, pH = 7.2, and ionic strength approximately 0.15. Neither P50 nor Hill's n showed any variation with hemoglobin concentrations increasing from 10 to 40 g/dl.
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Glycosylated hemoglobin is formed by a nearly irreversible reaction in which glucose becomes linked with hemoglobin. Glycosylated hemoglobin, hemoglobin A1, hemoglobin A1C, and fast hemoglobin all refer to this posttranslational modification of hemoglobin by the addition of a glucose moiety. The proportion of hemoglobin that is glycosylated is dependent primarily on the age of the RBC and the quantity of glucose to which it is exposed. Once formed, glycosylated hemoglobin remains in the erythrocyte for the duration of its life span. Assuming that RBC survival is 120 days, about 6% to 8% of hemoglobin is glycosylated in normoglycemic individuals, and 10% to 17% or more of hemoglobin will exist in the glycosylated form in hyperglycemic subjects. The glycosylation process is so slow that glycosylated hemoglobin measurements do not vary with minute-to-minute changes in blood glucose concentrations, but are believed to reflect a composite of all glucose levels that
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A simple, rapid method for the determination of the benzodiazepines, diazepam and chlordiazepoxide, and their metabolites by high performance liquid chromatography (HPLC) has been developed. The procedure is applicable to the assay of other similar drugs in biological fluids. The method utilizes BondElut™ extraction columns to facilitate the extraction. BondElut columns selectively adsorb the benzodiazepines and metabolites from serum at a pH of 9.0. The compounds are eluted with 300μl of methanol which makes sample concentration rapid, if even necessary. Analysis is performed using isocratic reversed-phase chromatography, and quantitation is carried out by ultraviolet (UV) detection. Using this procedure, it is possible to determine drug and metabolite levels to as low as 25 ng/ml in 0.5 ml of serum.
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In order to study the effect of hydrogen peroxide(H2O2)on the hemoglobin release of normal human red blood cell(RBC),The malondialdehyde contents and relative solubility of RBC and hemoglobin release test(HRT)were used to study the hemoglobin release of normal RBCs treated with different concentration(8%,4%,2%,1%,0.5%,0.25%and 0.125%)of H2O2.The results show that the hemoglobin release was increased with increased concentration of H2O2.However,high concentration of H2O2could decrease the released Hb.So different concentrations of H2O2has different effect on the hemoglobin release of RBC.
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