Results of routine determination of clinically significant hemoglobin derivatives by multicomponent analysis.

Abstract Our recently developed multiwavelength method for multi-component analysis of hemoglobin (Hb) derivatives (Clin Chem 1984;30:373-379) was adapted for routine use in the clinical chemical laboratory. The method was applied in 4066 determinations on blood specimens from patients awaiting major surgery (n = 3863) or visiting the outpatient department for pulmonary disease (n = 203). Mean total hemoglobin concentration was 141 (SD 14) g/L. The proportion of HbCO was slightly to moderately increased (1.5-10.0%) in 36.5% of all patients; in a few cases it was as high as 15%. Mean methemoglobin was 0.4% (SD 0.2%) in the surgical patients, but 1.5% (SD 0.8%) in the patients with pulmonary disease. In some patients of the latter group the proportion of methemoglobin amounted to 5%. Sulfhemoglobin was found less than 0.4% in all specimens. Interference by paraproteins and by increased concentrations of bilirubin and lipids in plasma was easily detected by means of the performance checks provided by the spectrophotometer (an HP 8451 UV/Vis). The method is equally suitable for measuring blood samples containing fetal hemoglobin.

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Molar absorptivities of human hemoglobin in the visible spectral range

Journal of Applied Physiology ◽

10.1152/jappl.1983.54.5.1287 ◽

1983 ◽

Vol 54 (5) ◽

pp. 1287-1291 ◽

Cited By ~ 37

Author(s):

W. G. Zijlstra ◽

A. Buursma ◽

A. Zwart

Keyword(s):

Human Blood ◽

Hemoglobin Concentration ◽

Visible Spectral Range ◽

Human Hemoglobin ◽

Spectrophotometric Methods ◽

Total Hemoglobin ◽

Wide Range ◽

Different Types ◽

Total Hemoglobin Concentration

In a recent paper, Burkhard and Barnikol (J. Appl. Physiol.: Respirat. Environ. Exercise Physiol. 52: 124–130, 1982) claimed that the absorption spectra of human (oxy-)hemoglobin are dependent on the total hemoglobin concentration (CHb) and it is suggested that this might also be the case with cyanmethemoglobin (HiCN). Such relationships would invalidate the widely used spectrophotometric methods for the determination of total hemoglobin and the fractions of various hemoglobin derivatives in human blood. Although Burkhard and Barnikol's findings are rather improbable considering earlier data, we measured the millimolar absorptivities of oxyhemoglobin (epsilon HbO2) and cyanmethemoglobin (epsilon HiCN) at various wavelengths over a wide range of concentrations (CHb approximately equal to 0.004–10 mmol x 1(-1)), using two different types of spectrophotometers. epsilon HbO2 and epsilon HiCN proved to be independent of CHb. Moreover the values obtained confirmed those in the earlier literature, whereas those of Burkhard and Barnikol are some 30% higher. Consequently there is no reason to doubt the validity of the generally accepted millimolar absorptivities of human hemoglobin.

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Interference of fetal hemoglobin and labile glycosylated hemoglobin with measurements of glycosylated hemoglobin.

Clinical Chemistry ◽

10.1093/clinchem/29.3.543 ◽

1983 ◽

Vol 29 (3) ◽

pp. 543-545 ◽

Cited By ~ 16

Author(s):

R W Yatscoff ◽

G J Tevaarwerk ◽

C L Clarson ◽

L M Warnock

Keyword(s):

Glycosylated Hemoglobin ◽

Accurate Determination ◽

Fetal Hemoglobin ◽

Hemoglobin Concentration ◽

Exchange Chromatography ◽

Affinity Column ◽

Affinity Column Chromatography ◽

Hemoglobin A1 ◽

Total Hemoglobin Concentration

Abstract We examined the effect of fetal hemoglobin and labile glycosylated hemoglobin on a number of diverse methods used to measure glycosylated hemoglobin. Samples were supplemented with various amounts of cord blood to give proportions of fetal hemoglobin ranging from 1 to 20% of total hemoglobin concentration. Procedures in which the separation of hemoglobin A1 from the major hemoglobin A fraction is based on differences in ionic properties (cation-exchange chromatography and electrophoresis) are subject to interference by fetal hemoglobin, whereas procedures that base the quantitation on other properties (colorimetry and affinity column chromatography) are not. The same procedures that are affected by the presence of fetal hemoglobin are also subject to interference by labile glycosylated hemoglobin. We conclude that the affinity chromatographic and colorimetric methods may give a more nearly accurate determination of glycosylated hemoglobin.

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Oxygen affinity of blood in altitude Sherpas

Journal of Applied Physiology ◽

10.1152/jappl.1979.47.2.337 ◽

1979 ◽

Vol 47 (2) ◽

pp. 337-341 ◽

Cited By ~ 44

Author(s):

M. Samaja ◽

A. Veicsteinas ◽

P. Cerretelli

Keyword(s):

Sea Level ◽

Concentration Ratio ◽

Oxygen Affinity ◽

Hemoglobin Concentration ◽

Cell Counts ◽

Blood Cell Counts ◽

Total Hemoglobin ◽

The Mean ◽

Total Hemoglobin Concentration ◽

2,3 Dpg

Oxygen equilibrium curves on blood within 6 h from sampling have been estimated from polarographic measurements of oxyhemoglobin concentration, in 13 male 14- to 50-yr old Sherpas residing at 3,850 m above sea level (Kumjung, Nepal). In samples with red blood cell counts = 4.7 +/- 0.8 (SD) x 10(6)/mm3, total hemoglobin concentration [Hb] = 17.0 +/- 1.9 g/dl, and hematocrit = 53.3 +/- 5.0, the mean oxygen half-saturation of hemoglobin (P50) (pH = 7.4 and PCO2 = 40 Torr) was 27.3 +/- 1.8 Torr. The P50 of altitude Sherpas was not significantly different from that of acclimatized lowlanders (28.2 +/- 1.3; n = 7), sea-level Caucasian residents (26.5 +/- 1.0; n = 17), and Sherpas at sea level (27.1; n = 3). The 2,3-diphosphoglyceric acid-to-hemoglobin concentration ratio ([2,3-DPG]/[Hb]) in altitude Sherpas was 1.22 +/- 0.03, the same as that of acclimatized Caucasians (1.22 +/- 0.10). The Bohr effect measured for the blood of one altitude Sherpas by the ratio deltalog P50/deltapH was -0.32 and -0.45 at PCO2 levels of 40 and 20 Torr, respectively. These values are not significantly different from those found in Caucasians at sea level where deltalog P50/deltalpH was -0.35 and -0.42, respectively. It is concluded that the P50 in native highlanders is not significantly different from that observed in sea-level dwellers. [2,3-DPG]/[Hb] at altitude, both in natives and in newcomers, is 20% higher than in sea-level residents.

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