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Digitale Medien

Microheterogeneity of bovine myelin basic protein studied by nuclear magnetic resonance spectroscopy (1983)

Deber, Charles M. ; Cheifetz, Sela ; Moscarello, Mario A.

New York : Wiley-Blackwell

Biopolymers 22 (1983), S. 377-380

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Details

ISSN: 0006-3525

Schlagwort(e): Chemistry ; Polymer and Materials Science

Quelle: Wiley InterScience Backfile Collection 1832-2000

Thema: Chemie und Pharmazie

Notizen: 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 1H-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.

Zusätzliches Material: 1 Ill.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1002/bip.360220148

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