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THE P 2 PROTEIN OF BOVINE ROOT MYELIN: ISOLATION AND SOME CHEMICAL AND IMMUNOLOGICAL PROPERTIES 1
Author(s) -
Brostoff S. W.,
Sacks H.,
Canto M. Dal,
Johnson A. B.,
Raine C. S.,
Wisniewski H.
Publication year - 1974
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.1471-4159.1974.tb10756.x
Subject(s) - myelin basic protein , myelin , biochemistry , major basic protein , antigen , chemistry , proteolipid protein 1 , polyacrylamide gel electrophoresis , central nervous system , biology , microbiology and biotechnology , immunology , enzyme , endocrinology , eosinophil , asthma
— A small basic protein (mol.wt. 12,000), referred to as the P 2 protein, was extracted with dilute acid from delipidated bovine root myelin and purified by ion exchange chromatography on cellulose phosphate. It appeared homogeneous on polyacrylamide gel electrophoresis. The P 2 protein had a distinctly different amino acid composition than the larger basic protein (mol.wt. 18,000), referred to as the P 1 protein, that is also present in peripheral nerve myelin. It contained relatively more hydrophobic residues and much less histidine and proline. The P 2 protein conjugated with peroxidase was bound by lymph node cells and infiltrates in rabbits sensitized with whole bovine root myelin. No binding was evident with the bovine central nervous system myelin basic protein. Chemically and immunologically, the P 2 protein appears to be specific to peripheral nervous system myelin. The isolated P 2 protein produced mild clinical symptoms of experimental allergic neuritis, but no histological evidence of disease. It was suggested that the P 2 protein is an important antigen for experimental allergic neuritis, and that its antigenic determinants are likely to be conformation‐dependent.