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JBC, Vol. 251, Issue 9, 2671-2679, May, 1976
F. C. Chou, C. H. Chou, R. Shapira and R. F. Kibler
The basic protein of bovine central nervous system myelin contains a single
polypeptide chain of 170 amino acids. Multiple components of basic protein
have been observed on disc gel electrophoresis and ion exchange
chromatography at alkaline pH, but the basis of the microheterogeneity has
not been established. In the present study myelin basic protein from bovine
spinal cord was chromatographed on carboxymethylcellulose at pH 10.4 in
glycine buffer/2 M urea. Three major peaks were obtained, identified as
components 4, 5, and 6 in the oder of their elution from the column by a
linear salt gradient. The amino acid compositions of tryptic peptides from
components 4 and 6 were identical and the COOH-terminal sequence,
Ala-Arg-Arg, was intact for all three components. Component 4 was found to
differ from component 6 by partial phosphorylation of threonine 98 and
serine 165. This modification was estimated to account for 50% of component
4. Component 5 differed from component 6 by partial deamidation of
glutamine residues 103 and 147, which accounted for 80% of this component.
These modified glutamine residues were also present in component 4 and
constituted another 15% of this component. It was considered that component
6 was the native, unmodified species of basic protein and that component 4
differed by a net negative charge of 2, and component 5 by a net negative
charge of.1 as a result of these modifications. The nonrandom nature of the
modifications suggested the involvement of specific enzymes.
Basis of microheterogeneity of myelin basic protein
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