Abstract:
:Using SDS-PAGE and MALDI-TOF mass spectrometry, we investigated the difference in the molecular structure between human and bovine ceruloplasmin. In both cases, we found that the protein is present in two majors forms of different molecular mass. The difference between human and bovine ceruloplasmin was more obvious when characterized by MALDI-TOF than with the SDS-PAGE analysis. Furthermore, we established that the N-glycoside content of both enzymes is dissimilar and that the N-glycosyl moieties are distributed in a distinctive fashion in two glycoproteins. Finally, it appeared that both proteins exhibited different cleavage patterns after treatment with trypsin. This study indicates that human and bovine ceruloplasmin differ not only in sugar composition but also in primary structure.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Boivin S,Aouffen M,Fournier A,Mateescu MAdoi
10.1006/bbrc.2001.5881subject
Has Abstractpub_date
2001-11-09 00:00:00pages
1006-10issue
4eissn
0006-291Xissn
1090-2104pii
S0006-291X(01)95881-4journal_volume
288pub_type
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