Abstract
Myelin was isolated from the brain of a coelacanth. Its protein components were separated by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate (SDS-PAGE). A protein component of 25000 Dalton was predominant; it was not glycosylated but reacted moderately with anti-mammalian CNS myelin proteolipid protein (PLP) antibodies and weakly with anti-lungfish CNS myelin glycosylated proteolipid protein (gPLP) antibodies. A component equivalent to mammalian DM-20 was not detectable. Presumably due to autolysis myelin basic protein (MBP) was not discernible by protein staining but showed up as a single band of 17000 Dalton with anti-mammalian MBP antibodies. Wolfgram protein (WP) was not present upon immunoblotting and the values for the myelin-specific 2′, 3′-cyclic nucleotide 3′-phosphodiesterase (CNPase) were extremely low. These results question a chondrichthyan association of the coelacanth but are strongly in favor of an Actinistia-Tetrapoda sister group relationship, with Dipnoi being most closely related to that combined group.
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Waehneldt, T.V., Malotka, J., Jeserich, G., Matthieu, JM. (1991). Central nervous system myelin proteins of the coelacanth Latimeria chalumnae: phylogenetic implications. In: Musick, J.A., Bruton, M.N., Balon, E.K. (eds) The biology of Latimeria chalumnae and evolution of coelacanths. Developments in environmental biology of fishes, vol 12. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3194-0_8
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