The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites.
Open accessAbstract
Nonenzymatic glycosylation of albumin in vivo occurs at multiple sites. Glucose gets attached to Lys-199, Lys-281, Lys-439, and Lys-525 as well as to some other lysine residues. The principal glycosylated site is Lys-525. Approximately 33% of the overall glycosylation occurs at this site. This site specificity is remarkable and is postulated to be a consequence of local catalysis of the nonenzymatic glycosylation reaction. It appears that positively charged amino groups in the protein catalyze the Amadori rearrangement at specific sites. The principal glycosylated site, Lys-525, lies in a Lys-Lys sequence; other glycosylated sites lie in a Lys-Lys, Lys-His, and Lys-His-Lys sequence or are near disulfide bridges, which are likely to place amino groups of more remote parts of the protein closer to these sites. The occurrence of nonenzymatic glycosylation at most of the identified sites in albumin from diabetic patients is explained by the concept of local acid-base catalysis of the Amadori rearrangement.
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Cites
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Nonenzymatic Glycosylation and the Pathogenesis of Diabetic Complications
BROWNLEE, M., VLASSARA, H., & CERAMI, A. (1984) · Annals of Internal Medicine · doi:10.7326/0003-4819-101-4-527 · Cited by 1,007
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Sites of nonenzymatic glycosylation of human hemoglobin A.
Shapiro, R., McManus, M. J., Zalut, C., & Bunn, H. F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85860-x · Cited by 368
Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum.
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The principal site of nonenzymatic glycosylation of human serum albumin in vivo.
Garlick, R. L., & Mazer, J. S. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32384-6 · Cited by 316
Non-enzymatic glycosylation and the chronic complications of diabetes: an overview
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Mutarotation, Hydrolysis, and Rearrangement Reactions of Glycosylamines1
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Cited by
Advanced Glycation End Products and Diabetic Complications
Singh, V. P., Bali, A., Singh, N., & Jaggi, A. S. (2014) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2014.18.1.1 · Cited by 1,518
Chou, T.-Y., Hart, G. W., & Dang, C. V. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18961 · Cited by 453
The glycation of albumin: Structural and functional impacts
Rondeau, P., & Bourdon, E. (2011) · Biochimie · doi:10.1016/j.biochi.2010.12.003 · Cited by 433
Clinical impact of glycated albumin as another glycemic control marker
Koga, M., & Kasayama, S. (2010) · Endocrine Journal · doi:10.1507/endocrj.k10e-138 · Cited by 290
Fructose-mediated non-enzymatic glycation: sweet coupling or bad modification
Schalkwijk, C. G., Stehouwer, C. D. A., & van Hinsbergh, V. W. M. (2004) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.488 · Cited by 206
Metadata
- Authors
- Iberg, N., & Flückiger, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-10
- Volume
- 261
- Issue
- 29
- Pages
- 13542-13545
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1499495082
- Cited by
- 379
- References
- 13
- FWCI
- 5.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Iberg, N., & Flückiger, R. (1986). Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)67052-8
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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