Glycosylated hemoglobin A1 in a random group of adult onset diabetics of indian subpopulation

1992 ◽  
Vol 7 (2) ◽  
pp. 138-142
Author(s):  
Tangirala Malati ◽  
D. Murali Mohan Krishna ◽  
V. R. Srinivasan ◽  
V. Shantharam
1982 ◽  
Vol 28 (1) ◽  
pp. 96-99 ◽  
Author(s):  
O Wålinder ◽  
G Ronquist ◽  
P J Fager

Abstract We compared a spectrophotometric kit method (Glycospec) for determination of glycosylated hemoglobin (HbA1) with a microcolumn kit method (Bio-Rad). The Glycospec method is based on the change in absorbance when phytic acid binds to hemoglobin A. With glycosylated hemoglobin there is no such change because the binding is blocked by the sugar moiety. Inter-assay CVs were 2-6% for both methods. In healthy subjects the mean (+/- SD) value for HbAl was about 1% higher with the spectrophotometric than the microcolumn method. For samples from 122 diabetics the correlation between values for HbAl obtained with the two methods was acceptable (r = 0.89), although the spectrophotometric technique yielded 2-4% higher values, a difference at least partly due to the absence of 2,3-diphosphoglycerate from the spectrophotometric standards. Adding 1.8 mmol of it per liter to these standards caused displacement of the standard curve; HbAl values then agreed well with those of the microcolumn method. The spectrophotometric procedure is easily automated, and therefore is well suited for large-scale analyses if problems with standards and calibration can be solved.


Blood ◽  
1980 ◽  
Vol 56 (3) ◽  
pp. 571-572 ◽  
Author(s):  
C Tegos ◽  
E Beutler

Abstract Partially purified hemoglobin A2 has been examined for the existence of glycosylated components by isoelectric focusing and by acid agar gel electrophoresis. Bands analogous to the glycohemoglobin derivatives of hemoglobin A, hemoglobin-A1.a.b.c, were readily detected. Evidence that these minor bands are in fact glycohemoglobins was obtained by showing that 14C-glucose bound to hemoglobin A2 moved with these minor bands. The amounts of glycohemoglobin derivatives of hemoglobin A2 were increased in the blood of diabetic patients.


Blood ◽  
1980 ◽  
Vol 56 (3) ◽  
pp. 571-572
Author(s):  
C Tegos ◽  
E Beutler

Partially purified hemoglobin A2 has been examined for the existence of glycosylated components by isoelectric focusing and by acid agar gel electrophoresis. Bands analogous to the glycohemoglobin derivatives of hemoglobin A, hemoglobin-A1.a.b.c, were readily detected. Evidence that these minor bands are in fact glycohemoglobins was obtained by showing that 14C-glucose bound to hemoglobin A2 moved with these minor bands. The amounts of glycohemoglobin derivatives of hemoglobin A2 were increased in the blood of diabetic patients.


1981 ◽  
Vol 27 (7) ◽  
pp. 1261-1263 ◽  
Author(s):  
D M Nathan

Abstract The utility of glycosylated hemoglobin (HbA1) measurement as an index of chronic control in diabetes can be adversely affected by interference from a labile glycosylated fraction that changes rapidly with acute changes in blood glucose concentration. I used a "high-pressure" liquid-chromatographic assay and a newly developed electrophoretic assay to quantitate the contribution of this labile fraction. If erythrocytes are incubated at 22 degrees C in isotonic saline for 12 h before hemolysis, the labile fraction is eliminated. Its contribution is similar as measured by both assays: 2-3.5% of total HbA1 in normal cells and 7-9.5% in diabetic cells. A 3-h incubation of erythrocytes with glucose produces acute changes in apparent HbA1 concentrations by both assays, but such changes can be eliminated by the incubation in saline. Although current methods are time consuming, the labile glycosylated hemoglobin must be removed when the sample is prepared for HbA1 measurement by liquid chromatography and electrophoresis if results are not to be factitiously high.


Stroke ◽  
2013 ◽  
Vol 44 (8) ◽  
pp. 2134-2138 ◽  
Author(s):  
A. Rocco ◽  
P. U. Heuschmann ◽  
P. D. Schellinger ◽  
M. Kohrmann ◽  
J. Diedler ◽  
...  

1982 ◽  
Vol 28 (3) ◽  
pp. 512-515 ◽  
Author(s):  
D M Nathan ◽  
E Avezzano ◽  
J L Palmer

Abstract The irreversible formation of stable glycosylated hemoglobin proceeds through a labile intermediate that is indistinguishable, by most methods, from the stable glycosylated product. The inclusion of the labile intermediate, which changes acutely with acute blood glucose changes, detracts from the utility of the assay as an index of chronic glucose concentration. We have developed a rapid, reliable chemical method for eliminating the labile intermediate: a 30-min incubation of whole-blood samples with semi-carbazide (30 mmol/L) and aniline (12 mmol/L) at pH 5 and 38 degrees C. The semicarbazide serves as a glucose trap; the transfer of glucose from the labile glycosylated hemoglobin to the semicarbazide is catalyzed by the acidic pH and aniline. This treatment is effective in the three most commonly used assays: "high-performance" liquid chromatography, electrophoresis, and a minicolumn kit.


1991 ◽  
Vol 6 (1) ◽  
pp. 51-57 ◽  
Author(s):  
Tangirala Malati ◽  
D. Murali Mohan Krishna ◽  
B. Sadasivudu

1980 ◽  
Vol 26 (11) ◽  
pp. 1598-1602 ◽  
Author(s):  
L Menard ◽  
M E Dempsey ◽  
L A Blankstein ◽  
H Aleyassine ◽  
M Wacks ◽  
...  

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