Comparison of a colorimetric assay for glycosylated hemoglobin with ion-exchange chromatography

Diabetes ◽  
1979 ◽  
Vol 28 (12) ◽  
pp. 1120-1125 ◽  
Author(s):  
R. E. Pecoraro ◽  
R. J. Graf ◽  
J. B. Halter ◽  
H. Beiter ◽  
D. Porte
Keyword(s):  
Ion Exchange ◽  
Colorimetric Assay ◽  
Glycosylated Hemoglobin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

Comparison of a Colorimetric Assay for Glycosylated Hemoglobin with Ion-exchange Chromatography

Diabetes ◽  
1979 ◽  
Vol 28 (12) ◽  
pp. 1120-1125 ◽  
Author(s):  
R. E. Pecoraro ◽  
R. J. Graf ◽  
J. B. Halter ◽  
H. Beiter ◽  
D. Porte
Keyword(s):  
Ion Exchange ◽  
Colorimetric Assay ◽  
Glycosylated Hemoglobin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

Glycated hemoglobin in uremic patients as measured by affinity and ion-exchange chromatography.

1984 ◽  
Vol 30 (3) ◽  
pp. 485-486 ◽  
Author(s):  
P Bannon ◽  
F Lessard ◽  
R Lepage ◽  
J G Joly ◽  
L Dufresne
Keyword(s):  
Ion Exchange ◽  
Chromatographic Method ◽  
Glycated Hemoglobin ◽  
Glycosylated Hemoglobin ◽  
Normal Subjects ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Significant Difference ◽  
Aminophenylboronic Acid ◽  
Uremic Patients

Abstract We estimated glycated ("glycosylated") hemoglobin in erythrocytes of hemodialyzed uremic patients by the aminophenylboronic acid affinity-chromatographic method and by an ion-exchange chromatographic method. As expected, apparent HbA1 concentrations were above normal in the uremic patients, owing to interference by the carbamylated hemoglobin. However, there was no significant difference between values for uremic and normal subjects when glycated hemoglobin was measured by the affinity method. Evidently it is unaffected by the presence of hemoglobin species modified by reactants not displaying a cis-1,2-diol group, such as carbamylated hemoglobin. For this reason it is preferable to the ion-exchange chromatographic method for accurate measurement of glycated hemoglobin.

Effects of whole blood storage on results for glycosylated hemoglobin as measured by ion-exchange chromatography, affinity chromatography, and colorimetry.

1983 ◽  
Vol 29 (6) ◽  
pp. 1113-1115 ◽  
Author(s):  
R R Little ◽  
J D England ◽  
H M Wiedmeyer ◽  
D E Goldstein
Keyword(s):  
Ion Exchange ◽  
Affinity Chromatography ◽  
Whole Blood ◽  
High Performance ◽  
Glycosylated Hemoglobin ◽  
Thiobarbituric Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Sample Collection ◽  
Sample Stability

Abstract After storage of whole blood at either 4 or 20 degrees C, results for glycosylated hemoglobin by ion-exchange chromatography ("high-performance" liquid and mini-column chromatography), thiobarbituric acid colorimetry, and affinity chromatography were compared. At 4 degrees C, all methods gave acceptable results for samples stored for as long as a week. At 20 degrees C, the colorimetric and affinity methods also showed sample stability for a week or more. The ion-exchange methods were associated with a marked increase in values for glycosylated hemoglobin after a few days of storage. Evidently, care in details of sample collection and handling is especially important for ion-exchange methods, and the colorimetric and affinity methods have advantages over ion exchange in situations where long delays between sample collection and assay are unavoidable.

Manual Determination of Intra-Erythrocytic 2,3-Diphosphoglycerate in Whole Blood by Enzymatic Analysis, and Comparison with Ion-Exchange Chromatography

1975 ◽  
Vol 21 (3) ◽  
pp. 376-380 ◽  
Author(s):  
James C Detter ◽  
Donald F Gibson ◽  
Stuart F MacMillan ◽  
Thomas H Oas
Keyword(s):  
Ion Exchange ◽  
Colorimetric Assay ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Single Subject ◽  
Enzymatic Analysis ◽  
Automated Method ◽  
Enzyme Method ◽  
Multiple Samples

Abstract A manual modification of an automated method [Atkinson, K. F., Clin. Chem. 18, 1001 (1972)] for enzymatic assay of 2,3-diphosphoglycerate is described, which is suitable for small laboratories. Samples are easily prepared for analysis, and preparations are stable for several months. Virtually all of the color generated in the colorimetric assay is produced by the diphosphoglycerate-catalyzed reaction. The coefficient of variation for multiple samples from a single subject was 2.4%. Delayed preparation of samples, particularly samples from some acidotic subjects, is shown to result in altered results. The enzyme method is compared with analysis by ion-exchange chromatography.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

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