✦ LIBER ✦

Microheterogeneity of bovine myelin basic protein studied by nuclear magnetic resonance spectroscopy

✍ Scribed by Charles M. Deber; Sela Cheifetz; Mario A. Moscarello

Publisher: Wiley (John Wiley & Sons)
Year: 1983
Tongue: English
Weight: 228 KB
Volume: 22
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360220148

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✦ Synopsis

Synopsis

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 '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.

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