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J. Biol. Chem., Vol. 259, Issue 8, 5028-5031, 04, 1984
BW Gibson, RD Gilliom, JN Whitaker and K Biemann
In order to resolve the uncertainties about the primary structure of human
myelin basic protein at residues 45-89, the sequence of this peptide and
its tryptic fragments were reinvestigated by fast atom bombardment mass
spectrometry. The sequence at positions 77-78 was found to be His-Gly and
the sequence at positions 83-84 was shown to be Glu-Asn. The Ser at
position 56 was not phosphorylated, whereas the residue at position 46 or
47 showed a heterogeneity of Gly and Ser in this peptide fragment in one of
two protein preparations from different patients. These results demonstrate
the usefulness of fast atom bombardment mass spectrometry for primary
structure information. The corrected sequence of human basic protein
peptide 45-89 will permit a more detailed immunochemical analysis of this
peptide and its in vivo degradation products.
Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry
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