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DISTRIBUTION AND OPTICAL ACTIVITY OF THE BASIC PROTEIN IN BOVINE PERIPHERAL NERVE MYELIN
Author(s) -
Uyemura K.,
KatoYamanaka T.,
Kitamura K.
Publication year - 1977
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1977.tb03924.x
Subject(s) - myelin , spinal cord , chemistry , myelin basic protein , circular dichroism , antiserum , peripheral nervous system , biochemistry , microbiology and biotechnology , central nervous system , biology , endocrinology , immunology , antibody , neuroscience
— Antiserum to BF protein isolated from bovine spinal roots has been used to study the distribution of the protein in other species and tissues. Significant amounts of protein could be demonstrated in bovine, pig and rabbit peripheral nerve myelin. It was, however, scarcely detectable in guinea pig peripheral nerve myelin. There was BF protein in rabbit spinal cord as well as in peripheral nerve, but little or no BF protein in the liver, kidney, muscle or brain. BF protein in bovine spinal cord was localized in the myelin. The ratio of the BF protein to the encephalitogenic protein in the spinal cord myelin was around 0.15:1.0. BF protein was extractable from peripheral nerve myelin by saline as well as by acid solutions. The circular dichroism spectrum of the BF protein in aqueous solution suggested that this protein contained a very large amount of β‐structure. This structure was not considered to be the result of acid denaturation because the protein purified from the saline extract of peripheral nerve also showed a similar spectrum.