Quantitation of Glycosylated Hemoglobin by Boronate Affinity Chromatography
Abstract
Total hemoglobin glycosylation and the contribution of glycosylation at the N-terminus of the beta-chains and at "non"-beta-N-terminal positions were quantitated by use of boronate affinity and ion exchange chromatography. Glycohemoglobin (y) was found to correlate linearly (y = 1.92x + 0.53; r = 0.96) with HbA1c (x) and to contain approximately 50% beta-N-terminally glycosylated hemoglobin. This result is in agreement with the binding on boronate agarose of the various hemoglobin components resolved by cation exchange chromatography. An amount of glycohemoglobin similar to that of HbA1c was isolatable from HbA. A slope of less than 2 results because HbA1c is retained only to 93% and the intercept of the regression line reflects the partial adherence (65%) of HbA1a + b to the resin. These results confirm the occurrence of significant "non"-beta-N-terminal glycosylation and show that under optimal chromatographic conditions total glycohemoglobin can be determined with boronate affinity chromatography.
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Boronate affinity chromatography is generally robust and less affected by hemoglobin variants, but its broader detection scope theoretically includes multiple glycated species beyond the IFCC-defined β-N-terminal glycation.
“Although this method is generally robust and less affected by hemoglobin variants, its broader detection scope theoretically includes multiple glycated species beyond the IFCC-defined β-N-terminal glycation (38,39).”
From Comparison of point‑of‑care HbA1c devices with laboratory HPLC methods: A systematic review and meta‑analysis (2026) · cites this paper as [38]
Boronate affinity chromatography targets cis-diol structures of glycated residues, regardless of glycation site.
“Boronate affinity chromatography, employed by devices such as Afinion and A1C EZ 2.0, targets cis-diol structures of glycated residues, regardless of glycation site (38).”
From Comparison of point‑of‑care HbA1c devices with laboratory HPLC methods: A systematic review and meta‑analysis (2026) · cites this paper as [38]
Cited by
Sorted by citations
Carnethon, M. R. (2005) · JAMA · doi:10.1001/jama.294.23.2981 · Cited by 417 · see citing works
Berg, A. H., & Sacks, D. B. (2008) · Journal of Clinical Pathology · doi:10.1136/jcp.2007.049205 · Cited by 41 · see citing works
Wei, Y., Gu, M., Ren, Y., & Hu, Z. (2026) · Biomedical Reports · doi:10.3892/br.2026.2120 · Cited by 3 · see citing works
“N‑terminal glycation (38,39).”
Influential
- Authors
- Flückiger, R., Woodtli, T., & Berger, W.
- Affiliations
- University Hospital of Basel (CH)
- ORCID
- Flückiger, Rudolf
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 1984-01-01
- Volume
- 33
- Issue
- 1
- Pages
- 73-76
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2153929626
- Cited by
- 87
- References
- 0
- Citations by year
- 2025: 2 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 3 · 2015: 4 · 2014: 2 · 2013: 6 · 2012: 3
- FWCI
- 1.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Management and Research
- Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
- Keywords
- HbA1c, boronate affinity chromatography, hemoglobin A, ion-exchange chromatography
- MeSH terms
- Borohydrides, Chromatography, Affinity, Chromatography, Ion Exchange, Glycated Hemoglobin
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