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Microheterogeneity of bovine myelin basic protein studied by nuclear magnetic resonance spectroscopy
Author(s) -
Deber Charles M.,
Cheifetz Sela,
Moscarello Mario A.
Publication year - 1983
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360220148
Subject(s) - chemistry , cationic polymerization , nuclear magnetic resonance spectroscopy , spectroscopy , myelin , sulfoxide , stereochemistry , organic chemistry , physics , quantum mechanics , neuroscience , biology , central nervous system
Myelin basic protein isolated from bovine white matter is known to consist of a mixture of three or more “charge isomers”, which can be separated by cation‐exchange chromatography. We are using 360‐MHz 1 H‐nmr spectroscopy to establish the chemical and structural differences among them. Preliminary studies by difference spectroscopy between two of the isomers suggest (a) all aromatic residues, and probably their nearest‐neighbors, are unchanged; (b) the less cationic isomer lacks one (or two) of its C‐terminal Arg residues; and (c) a significant fraction of the two Met residues in the less cationic isomer is present as methionine sulfoxide.