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Structural analysis of biologically active peptides and recombinant proteins and their modified counterparts by mass
B N Pramanik1, A Tsarbopoulos, J E Labdon
1Schering-Plough Research, Bloomfield, NJ 07003.
Journal of Chromatography
|January 2, 1991
Abstract:
The structural characterization of the Escherichia coli-expressed human interferon alpha-2b (rh-IFN alpha-2b) was carried out by employing the fast atom bombardment (FAB) and plasma desorption (PD) mapping methods. The mass spectral data of the rh-IFN alpha-2b and the trypsin-generated peptide mixture allowed rapid and facile confirmation of the cDNA-derived sequence and determination of the existing disulfide pattern in the protein molecule. The same PD/FAB mapping approach was successfully employed in the structural determination of the iodination reaction product of rh-IFN alpha-2b and the potent vasoconstrictor peptide endothelin.