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Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum.
Open accessAbstract
Incubation of human serum with D-[6-3H]glucose resulted in the gradual accumulation of radioactivity in acid-precipitable material. Upon chromatography on Sephadex G-200, radioactivity was found associated with each of the major molecular weight classes of serum protein. Purified human serum albumin was also glucosylated in vitro upon exposure to D-[6-3H]glucose in phosphate-buffered saline. The glucosylated and unmodified albumins were separated by ion exchange chromatography. The physiological significance of these observations in vitro was confirmed by the isolation and quantitation of glucosylated albumin from normal human serum. Glucosylated albumin represents approximately 6 to 15% of total serum albumin in normal adults. The post-translational modification appears to occur by a nonenzymatic process analogous to that responsible for glucosylation of hemoglobin A to hemoglobin AIc, i.e. through Schiff base formation and Amadori rearrangement to a ketoamine derivative.
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Cited by
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Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites.
Iberg, N., & Flückiger, R. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67052-8 · Cited by 379
Thornalley, P. J., & Rabbani, N. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.03.025 · Cited by 133
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Metadata
- Authors
- Day, J. F., Thorpe, S. R., & Baynes, J. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-02
- Volume
- 254
- Issue
- 3
- Pages
- 595-597
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1516138002
- Cited by
- 334
- References
- 0
- FWCI
- 14.89
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Day, J. F., Thorpe, S. R., & Baynes, J. W. (1979). Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)37845-6
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