Related Experiment Video
Updated: Sep 13, 2026

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
Published on: October 4, 2017
Primary sequence and glycation at lysine-548 of bovine serum albumin
1Department of Molecular Medicine, Osaka Medical Centre, Japan.
Abstract:
The cDNA sequence of bovine serum albumin (BSA) was analysed to confirm the amino acid residues that were not consistent among the current databases. Residues 42, 190, 214, 324, 394 were His, Glu, Thr, Asn, Ser and Thr, respectively, consistent with a database of accession number X58989. The sequencing results and the mass spectrometry of digested peptides of BSA from three different suppliers ruled out heterogeneity in the primary structure. Asn-324 was not deamidated. Thus, the molecular mass of this protein was 66429. Like its human albumin counterpart, Lys-548 of BSA was partially glycated. The collision-induced dissociation mass spectrum of the Amadori-rearranged sugar moiety is presented.
More Related Videos
Related Concept Videos
Globular and Fibrous Proteins
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Ligand Binding and Linkage
Protein Glycosylation
Glycosylation occurs in...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Folding Quality Check in the RER
Proteoglycans

