PROTEINS AND GLYCOPROTEINS IN MYELIN PURIFIED FROM THE DEVELOPING BOVINE AND HUMAN CENTRAL NERVOUS SYSTEMS

Myclin was purified from bovine and human midbrain at various stages of prenatal and postnatal development. Basic protein and proteolipid proteins were the major individual proteins at all stages. The specific activity of 2′3′-cyclic nucleotide 3′-phosphohydrolase remained constant in the bovine myclin during development but decreased slightly in human myelin. A high molecular weight glycoprotein with electrophoretic mobility similar to that previously reported in rodent myelin (QUARLES et al., 1973) was present in both bovine and human myelin at all stages of development. The intensity of staining of this glycoprotein with periodic acid-Schiff reagents per mg total myelin protein was less in mature bovine and human myelin than in rat myelin.