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Primary Sequence and Glycation at Lysine‐548 of Bovine Serum Albumin
Author(s) -
Wada Yoshinao
Publication year - 1996
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/(sici)1096-9888(199603)31:3<263::aid-jms292>3.0.co;2-2
Subject(s) - chemistry , bovine serum albumin , glycation , amadori rearrangement , protein primary structure , biochemistry , molecular mass , serum albumin , complete sequence , lysine , peptide sequence , chromatography , mass spectrometry , albumin , amino acid , enzyme , receptor , genome , gene
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.