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PMID: 6201481 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry.

The Journal of biological chemistry ·Vol. 259 ·No. 8 ·1984-04-25 ·Pages 5028-31

Gibson BW, Gilliom RD, Whitaker JN, Biemann K

Abstract

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.

MeSH Terms
Amino Acid Sequence Brain Chemistry Chromatography, High Pressure Liquid Humans Male Mass Spectrometry Myelin Basic Protein Peptide Fragments/analysis Trypsin
Chemicals
Myelin Basic Protein Peptide Fragments myelin basic protein 45-89 Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gibson B W
Gilliom R D
Whitaker J N
Biemann K
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1984-04-25
Pages
5028-31
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM05472 · United States
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