Investigation and validation of the affinity chromatography method for measuring glycated albumin in serum and urine
Affinity chromatography on m-aminophenyl boronate columns together with albumin measurement by radioimmunoassay has been validated as a method for determining glycated albumin in serum and urine. Optimisation of sample volume and of elution buffer composition and volume ensured reproducibility of re...
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| Published in | Clinica chimica acta Vol. 202; no. 1; pp. 11 - 22 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Shannon
Elsevier B.V
14.10.1991
Elsevier |
| Subjects | |
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| Abstract | Affinity chromatography on m-aminophenyl boronate columns together with albumin measurement by radioimmunoassay has been validated as a method for determining glycated albumin in serum and urine. Optimisation of sample volume and of elution buffer composition and volume ensured reproducibility of results. Fructosamine assay confirmed the absence of glycated albumin species from the non-glycated fraction. It was possible to elute the glycated fraction from the affinity columns with Tris or glycine which do not contain 1, 2 diols but have similar functional groups. Column affinity was, therefore, not specific for glycated protein moieties. Inhibition of binding by glucose, and other small molecules in urine, necessitated ultrafiltration or dialysis of samples before analysis. Reference ranges for glycated albumin in non-diabetic subjects were 0.6–1.8% in serum and 0.9–2.6% in urine. In patients with diabetes mellitus, glycated albumin ranged from 1.4–10.9% in serum and from 1.5–12.5% in urine. |
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| AbstractList | Affinity chromatography on m-aminophenyl boronate columns together with albumin measurement by radioimmunoassay has been validated as a method for determining glycated albumin in serum and urine. Optimisation of sample volume and of elution buffer composition and volume ensured reproducibility of results. Fructosamine assay confirmed the absence of glycated albumin species from the non-glycated fraction. It was possible to elute the glycated fraction from the affinity columns with Tris or glycine which do not contain 1,2 diols but have similar functional groups. Column affinity was, therefore, not specific for glycated protein moieties. Inhibition of binding by glucose, and other small molecules in urine, necessitated ultrafiltration or dialysis of samples before analysis. Reference ranges for glycated albumin in non-diabetic subjects were 0.6-1.8% in serum and 0.9-2.6% in urine. In patients with diabetes mellitus, glycated albumin ranged from 1.4-10.9% in serum and from 1.5-12.5% in urine. Affinity chromatography on m-aminophenyl boronate columns together with albumin measurement by radioimmunoassay has been validated as a method for determining glycated albumin in serum and urine. Optimisation of sample volume and of elution buffer composition and volume ensured reproducibility of results. Fructosamine assay confirmed the absence of glycated albumin species from the non-glycated fraction. It was possible to elute the glycated fraction from the affinity columns with Tris or glycine which do not contain 1,2 diols but have similar functional groups. Column affinity was, therefore, not specific for glycated protein moieties. Inhibition of binding by glucose, and other small molecules in urine, necessitated ultrafiltration or dialysis of samples before analysis. Reference ranges for glycated albumin in non-diabetic subjects were 0.6-1.8% in serum and 0.9-2.6% in urine. In patients with diabetes mellitus, glycated albumin ranged from 1.4-10.9% in serum and from 1.5-12.5% in urine.Affinity chromatography on m-aminophenyl boronate columns together with albumin measurement by radioimmunoassay has been validated as a method for determining glycated albumin in serum and urine. Optimisation of sample volume and of elution buffer composition and volume ensured reproducibility of results. Fructosamine assay confirmed the absence of glycated albumin species from the non-glycated fraction. It was possible to elute the glycated fraction from the affinity columns with Tris or glycine which do not contain 1,2 diols but have similar functional groups. Column affinity was, therefore, not specific for glycated protein moieties. Inhibition of binding by glucose, and other small molecules in urine, necessitated ultrafiltration or dialysis of samples before analysis. Reference ranges for glycated albumin in non-diabetic subjects were 0.6-1.8% in serum and 0.9-2.6% in urine. In patients with diabetes mellitus, glycated albumin ranged from 1.4-10.9% in serum and from 1.5-12.5% in urine. |
| Author | Lamb, Edmund Dawnay, Anne B.St.J. Silver, Anne C. Cattell, William R. |
| Author_xml | – sequence: 1 givenname: Anne C. surname: Silver fullname: Silver, Anne C. organization: Renal Research Laboratory, Departments of Chemical Pathology, St Bartholomew's Hospital, LondonU.K – sequence: 2 givenname: Edmund surname: Lamb fullname: Lamb, Edmund organization: Renal Research Laboratory, Departments of Chemical Pathology, St Bartholomew's Hospital, LondonU.K – sequence: 3 givenname: William R. surname: Cattell fullname: Cattell, William R. organization: Renal Research Laboratory, Departments of Nephrology, St Bartholomew's Centre for Clinical Research, St Bartholomew's Hospital, LondonU.K – sequence: 4 givenname: Anne B.St.J. surname: Dawnay fullname: Dawnay, Anne B.St.J. organization: Renal Research Laboratory, Departments of Chemical Pathology, St Bartholomew's Hospital, LondonU.K |
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| Cites_doi | 10.1016/S0009-9120(88)80005-5 10.1080/00032718108055476 10.1007/BF00253503 10.1093/clinchem/34.9.1906 10.1093/clinchem/33.12.2220 10.1016/0022-1902(70)80145-2 10.1093/clinchem/34.7.1456 10.1016/0009-8981(74)90357-X 10.1093/clinchem/32.7.1303 10.1016/0009-8981(86)90212-3 10.1021/ja01030a019 10.1177/000456328502200108 10.2337/diab.29.8.623 10.1093/clinchem/30.6.1111 10.1016/S0021-9258(19)69387-7 10.1093/clinchem/28.10.2088 10.1016/S0021-9258(17)43857-9 10.1021/bi00824a021 10.1177/000456328402100103 |
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| Keywords | Glycated albumin Glycated protein m-Aminophenyl boronate affinity chromatography Urine protein Human Urine Biological fluid Affinity chromatography Diabetes mellitus Radioimmunoassay Clinical biology Albumin Biological marker Serum Quantitative analysis |
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| References | Conroy, Simon, Demetriou (BIB19) 1984; 30 Neglia, Cohen, Garber, Ellis, Thorpe, Baynes (BIB12) 1983; 258 Silver, Dawnay, Landon, Cattell (BIB8) 1986; 32 Willey, Rosenthal, Caldwell (BIB14) 1984; 27 Austin, Mullins, Morin (BIB15) 1987; 33 Higgins, Bunn (BIB10) 1981; 256 Klenk, Hermanson, Krohn (BIB11) 1982; 28 John (BIB13) 1984; 30 Reed, Bhatnagar, Dhar, Winocour (BIB21) 1986; 161 Weith, Weibers, Gilham (BIB18) 1970; 9 John, Jones (BIB3) 1985; 22 Kustin, Pizer (BIB17) 1969; 91 Nickerson (BIB16) 1970; 32 Johnson, Baker (BIB5) 1988; 34 Webster, Bignell, Attwood (BIB7) 1974; 53 Woo, Sunderji, Ozark, Ennis (BIB20) 1985; 31 Morin, Austin, Mullins (BIB6) 1988; 21 Schaffer (BIB22) 1988; 34 Gould, Hall, Cook (BIB2) 1984; 21 Rendell, Kao, Mecherikunnel (BIB4) 1985; 105 Goldstein, Peth, England, Hess, da Costa (BIB9) 1980; 29 Mallia, Hermanson, Krohn, Fujimoto, Smith (BIB1) 1981; 14 Johnson (10.1016/0009-8981(91)90251-7_BIB5) 1988; 34 Nickerson (10.1016/0009-8981(91)90251-7_BIB16) 1970; 32 Reed (10.1016/0009-8981(91)90251-7_BIB21) 1986; 161 Webster (10.1016/0009-8981(91)90251-7_BIB7) 1974; 53 Morin (10.1016/0009-8981(91)90251-7_BIB6) 1988; 21 Higgins (10.1016/0009-8981(91)90251-7_BIB10) 1981; 256 Conroy (10.1016/0009-8981(91)90251-7_BIB19) 1984; 30 Neglia (10.1016/0009-8981(91)90251-7_BIB12) 1983; 258 John (10.1016/0009-8981(91)90251-7_BIB13) 1984; 30 Rendell (10.1016/0009-8981(91)90251-7_BIB4) 1985; 105 Goldstein (10.1016/0009-8981(91)90251-7_BIB9) 1980; 29 Silver (10.1016/0009-8981(91)90251-7_BIB8) 1986; 32 Woo (10.1016/0009-8981(91)90251-7_BIB20) 1985; 31 Klenk (10.1016/0009-8981(91)90251-7_BIB11) 1982; 28 Weith (10.1016/0009-8981(91)90251-7_BIB18) 1970; 9 Mallia (10.1016/0009-8981(91)90251-7_BIB1) 1981; 14 Gould (10.1016/0009-8981(91)90251-7_BIB2) 1984; 21 Willey (10.1016/0009-8981(91)90251-7_BIB14) 1984; 27 Austin (10.1016/0009-8981(91)90251-7_BIB15) 1987; 33 Schaffer (10.1016/0009-8981(91)90251-7_BIB22) 1988; 34 Kustin (10.1016/0009-8981(91)90251-7_BIB17) 1969; 91 John (10.1016/0009-8981(91)90251-7_BIB3) 1985; 22 |
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| SubjectTerms | Adult Albuminuria Analytical, structural and metabolic biochemistry Binding and carrier proteins Biological and medical sciences Biomarkers - blood Biomarkers - urine Chromatography, Affinity - methods Diabetes Mellitus - blood Diabetes Mellitus - urine Fructosamine Fundamental and applied biological sciences. Psychology Glycated albumin Glycated protein Glycosuria Glycosylation Hexosamines - blood Humans m-Aminophenyl boronate affinity chromatography Middle Aged Proteins Radioimmunoassay - methods Reference Values Serum Albumin - analysis Urine protein |
| Title | Investigation and validation of the affinity chromatography method for measuring glycated albumin in serum and urine |
| URI | https://dx.doi.org/10.1016/0009-8981(91)90251-7 https://www.ncbi.nlm.nih.gov/pubmed/1807865 https://www.proquest.com/docview/72699430 |
| Volume | 202 |
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