THE P2 PROTEIN OF BOVINE ROOT MYELIN: ISOLATION AND SOME CHEMICAL AND IMMUNOLOGICAL PROPERTIES

S. W. Brostoff*, H. Sacks, M. Dal Canto, A. B. Johnson, C. S. Raine, H. Wisniewski

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

52 Scopus citations

Abstract

Abstract— A small basic protein (mol.wt. 12,000), referred to as the P2 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 P2 protein had a distinctly different amino acid composition than the larger basic protein (mol.wt. 18,000), referred to as the P1 protein, that is also present in peripheral nerve myelin. It contained relatively more hydrophobic residues and much less histidine and proline. The P2 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 P2 protein appears to be specific to peripheral nervous system myelin. The isolated P2 protein produced mild clinical symptoms of experimental allergic neuritis, but no histological evidence of disease. It was suggested that the P2 protein is an important antigen for experimental allergic neuritis, and that its antigenic determinants are likely to be conformation‐dependent.

Original languageEnglish (US)
Pages (from-to)1037-1043
Number of pages7
JournalJournal of neurochemistry
Volume23
Issue number5
DOIs
StatePublished - Nov 1974

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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