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The intrinsic fluorescence characteristics of tyrosine and tryptophan residues in the proteins of isolated central-nervous-system myelin were investigated to gain information concerning the location of these residues within the intact membrane system. Tryptophan fluorescence from isolated myelin has an emission maximum at 325 nm that appears to arise from at least two different populations of tryptophan residues. Further evidence for heterogeneity of tryptophan location in the membrane is obtained from quenching studies with chloroform and acrylamide. It is speculated that one tryptophan population is hydrophobically situated and may be derived from the proteolipid protein of myelin, whereas the other tryptophan population is located at the membrane surface and may arise from the extrinsic basic protein. A significant tyrosine fluorescence is detected from isolated myelin, indicating that some of these residues are not quenched by structural interactions within the lipid--protein membrane system. Studies with freeze-dried resuspended myelin suggest that the structural arrangement of protein components in the dried rehydrated membrane system differs significantly from that of the freshly isolated myelin membrane.

The intrinsic fluorescence of isolated central-nervous-system myelin-sheath preparations