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Presence of Proteolipid Protein in Coelacanth Brain Myelin Demonstrates Tetrapod Affinities and Questions a Chondrichthyan Association
Author(s) -
Waehneldt T. V.,
Malotka J.
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb07281.x
Subject(s) - affinities , tetrapod (structure) , proteolipid protein 1 , biology , evolutionary biology , association (psychology) , zoology , myelin , anatomy , paleontology , neuroscience , psychology , myelin basic protein , central nervous system , biochemistry , psychotherapist
The protein and glycoprotein compositions of CNS myelin from the living coelacanth (Latimeria chalumnae) were analyzed by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. An unglycosylated component of 25 kilodaltons showed substantially stronger immunoblot reactivity with antibodies against mammalian proteolipid protein (PLP) than lungfish glycosylated PLP. DM‐20 (intermediate protein) was not detectable in either fish. The presence of unglycosylated PLP in CNS myelin of the actinistian coelacanth contradicts an association with cartilaginous fishes but supports tetrapod affinities closer than those of lungfish.