Characterisation of oligosaccharides from a glycoprotein variant of human serum albumin (albumin Casebrook) using high-performance anion-exchange chromatography and nuclear magnetic resonance spectroscopy.

doi:10.1016/0378-4347(92)80271-q

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Article

Characterisation of oligosaccharides from a glycoprotein variant of human serum albumin (albumin Casebrook) using high-performance anion-exchange chromatography and nuclear magnetic resonance spectroscopy.

Journal of chromatography - 23 Oct 1992

Haynes P A, Batley M, Peach R J, Brennan S O, Redmond J W

Abstract excerpt

The characterisation of oligosaccharides present on albumin Casebrook, a glycoprotein variant of human serum albumin, which contains an N-linked oligosaccharide at an attachment site formed by a point mutation of 494 Asp-->Asn, is described. The monosaccharide compositional analysis of purified g...

Topics

Amidohydrolases
Carbohydrate Sequence
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Glycoproteins
Humans
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Monosaccharides
Mutation
Oligosaccharides
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Serum Albumin

Source

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Identifiers

PMID: 1452609
DOI: 10.1016/0378-4347(92)80271-q

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1452609-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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