The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants.

doi:10.1016/j.bbagen.2003.08.001

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Article

The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants.

Biochimica et biophysica acta - 13 Oct 2003

Nakajou Keisuke, Watanabe Hiroshi, Kragh-Hansen Ulrich, Maruyama Toru, Otagiri Masaki

Abstract excerpt

Recombinant wild-type human serum albumin (rHSA), the single-residue mutants K199A, K439A and K525A and the triple-residue mutant K199A/K439A/K525A were produced using a yeast expression system. Portions of the rHSA were glycated to different degrees (2.5-250 mM D-glucose). As detected by far-UV and near-UV CD, intrinsic tryptophan-fluorescence and probed by 1,1'-bis(4-anilino)naphthalene-5,5-disulfonic acid, the...

Topics

Animals
Base Sequence
Binding Sites
Circular Dichroism
DNA, Recombinant
Esterases
Glycosylation
Humans
In Vitro Techniques
Ligands
Male

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Mutagenesis, Site-Directed

Mutation

Protein Conformation

Rats

Rats, Wistar

Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 14572906
DOI: 10.1016/j.bbagen.2003.08.001

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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