The overall purpose of the present study is an understanding of the chemical architecture of the brain and the relationships between its protein and lipid components. Primary emphasis is placed on the chemistry of myelin proteins. During the coming year the major effort will be difected towards the long range goal of determiningthe amino acid sequence of proteolipid protein from bovine brain white matter (myelin proteolipid). We plan to 1) continue to purify and sequence the peptides which we have obtained by tryptic digestion and by elastase digestion 2) develop procedures for using high pressure liquid chromatography for the purification of peptides, particularly hydrophobic peptides, which are difficult to separate by conventional column chromatography 3) develop procedures for the reductive alkylation of the proteolipid apoprotein. 4) We have recently been able to demonstrate that we have purified antibodies to the bovine white matter apoprotein. An additional line of investigation will involve a characterization of the immunological properties of the apoprotein. These studies address fundamental problems related to myelin and should contribute to an understanding of the normal process of myelination and the abnormalities which occur in demyelinating diseases including multiple sclerosis and disease of genetic and environmental origin.