Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Diabetes Care ; 10(5): 629-32, 1987.
Article in English | MEDLINE | ID: mdl-3677984

ABSTRACT

We have developed techniques that permit the affinity-chromatographic determination of glycosylated hemoglobin, plasma protein, and albumin on fingerstick samples of whole blood. The fingerstick glycohemoglobin technique takes advantage of the high sensitivity of measurement of hemoglobin by absorbance at 414 nm. The glycosylated plasma protein is assayed by a highly sensitive method based on binding of Coomassie blue. An enzyme-linked immunosorbent assay is used to measure albumin in the bound and nonbound fractions of an aminophenylboronic acid chromatographic separation. The fingerstick method for assay of glycosylated plasma albumin gives results that are approximately 40% higher than comparable values obtained on the same patient with a 1-ml plasma sample determined with the bromcresol green technique. There is good correlation of fingerstick glycoalbumins with fingerstick glycohemoglobins and glycosylated plasma protein values. These procedures should be useful for children and for large-scale ambulatory screening for diabetes mellitus.


Subject(s)
Blood Proteins/analysis , Diabetes Mellitus/blood , Glycated Hemoglobin/analysis , Glycoproteins , Serum Albumin/analysis , Blood Chemical Analysis/methods , Blood Specimen Collection/methods , Glycation End Products, Advanced , Glycosylation , Humans , Glycated Serum Proteins , Glycated Serum Albumin
2.
Comp Biochem Physiol B ; 81(4): 819-22, 1985.
Article in English | MEDLINE | ID: mdl-4042626

ABSTRACT

Aminophenylboronic acid affinity chromatography was used to measure glycosylated hemoglobin and glycosylated albumin levels in a variety of species. The highest glycosylated hemoglobin levels were found in man, the lowest in the chicken and the pig. The highest glycosylated albumin levels were found in avian species, the lowest in the mouse and the rat. A simple kinetic model was used to analyze the rates of formation of glycosylated hemoglobin and albumin in the various species. Rates of glycosylated albumin formation were very similar across the species while rates of glycosylated hemoglobin formation were quite different, presumably reflecting wide differences in erythrocyte permeability to glucose among the species.


Subject(s)
Glycated Hemoglobin/analysis , Serum Albumin/analysis , Animals , Blood Glucose/metabolism , Chromatography, Affinity , Dogs , Erythrocytes/metabolism , Glycated Hemoglobin/biosynthesis , Glycation End Products, Advanced , Humans , Mice , Rabbits , Rats , Serum Albumin/biosynthesis , Species Specificity , Glycated Serum Albumin
SELECTION OF CITATIONS
SEARCH DETAIL
...