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Primary Sequence and Glycation at Lysine-548 of Bovine Serum Albumin

✍ Scribed by Wada, Yoshinao

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
334 KB
Volume
31
Category
Article
ISSN
1076-5174

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✦ Synopsis

The cDNA sequence of bovine serum albumin (BSA) was analysed to confirm the amino acid residws 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. Thns, 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.

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