Biological variation in glycated proteins.
The high degree of individuality in the fructosamine assay has been ascribed to non-specific interferences in the assay. To investigate this, we measured the biological variability of 10 non-diabetic subjects using the fructosamine assay, the new fructosamine plus assay, glycated albumin and glycated total plasma proteins by affinity chromatography. The total variation of the two fructosamine assays was half that of the affinity chromatography assays. This was mainly due to the greater analytical imprecision of the affinity chromatography assays. The resulting high index of heterogeneity for both affinity methods makes it difficult to assess the significance of changes in serial results. The within-subject variation made a small contribution to the total variation for all the assays, and was particularly low for the fructosamine assays. This suggests that any non-specific component makes a constant contribution to the measured fructosamine activity in non-diabetic subjects. The fructosamine assays therefore have significant advantages over the affinity chromatography methods as indices of medium-term glycaemic control.
Department of Biochemistry, Kingston Hospital, Kingston-Upon-Thames, Surrey, UK.
S J
SJ
Davie
K L
KL
Whiting
B J
BJ
Gould
D000293:Adolescent; D000328:Adult; D001798:Blood Proteins / Q000032:analysis*; D002846:Chromatography, Affinity; D005260:Female; D019270:Fructosamine; D017127:Glycation End Products, Advanced; D006031:Glycosylation; D006595:Hexosamines / Q000097:blood*; D006801:Humans; D008297:Male; D012709:Serum Albumin / Q000032:analysis*; D000093423:Glycated Serum Albumin
D001798:Blood Proteins; D017127:Glycation End Products, Advanced; D006595:Hexosamines; D012709:Serum Albumin; D019270:Fructosamine; D000093423:Glycated Serum Albumin