By comparison to the large amount of work that has been carried out on myelin lipids in health and in disease, scanty attention has been paid until recently to myelin proteins. Indeed what was known about central myelin proteins in the late fifties had been surmised from the differences in composition between central gray and white matters, and from the changes in composition during maturation of the central nervous system. It could have been summarized by stating that neurokeratin (8), and the then recently recognized proteolipids (12) were most likely components of central myelin. Neurokeratin was the gastric juice, pancreatic juice resistant fraction of defatted brain proteins. Its occurrence had been known for almost a century, and in the fifties it had been prepared by improved methods as a trypsin-resistant protein residue (TRPR) (24). Proteolipids were a group of protein-lipid complexes that had been isolated from brain tissue in 1951, and which had the property of being insoluble in aqueous solutions, and soluble in chloroform-methanol mixtures (12). TRPR and proteolipids were obtained in parallel from a single tissue sample by extraction with chloroform-methanolthe extract contained the proteolipids, and TRPR was obtained by tryptic digestion of the chloroform-methanol insoluble tissue residue. The two materials were similar in amino acid composition, in their insolubility in aqueous solutions, and in being resistant to the action of most proteolytic enzymes. This left, as main difference between the two, the insolubility of TRPR in chloroform-methanol as compared to the ready solubility of proteolipids in the same solvent mixtures.


Amino Acid Composition Silicic Acid Biphasic System Proteolipid Protein Acidic Lipid 
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Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • J. Folch-Pi
    • 1
    • 2
  1. 1.Harvard Medical SchoolBostonUSA
  2. 2.McLean HospitalBelmontUSA

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