A glycosylated proteolipid protein is common to CNS myelin of recent lungfish (Ceratodiae, Lepidosirenidae)

T. V. Waehneldt*, J. M. Matthieu, J. Malotka, J. Joss

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

1. 1. Myelin proteins from the CNS of recent lungfish (Lepidosiren paradoxa, Protopterus dolloi, Neoceratodus forsteri) were separated and analysed by staining and immunoblotting. 2. 2. All species showed a glycosylated component (g-PLP) that cross-reacted with antibodies against tetrapod proteolipid protein (PLP), indicating phylogenetic relationships with amphibia. 3. 3. Actinopterygian IP or teleostean 36 k components were not detectable in lungfish CNS myelin. 4. 4. The identical size of g-PLPs from Lepidosiren and Protopterus (Mr = 29,000) underlines the close relationship of the Lepidosirenidae. The smaller size of g-PLP from the ceratodidan Neoceratodus forsteri (Mr = 27,500) pointed to an earlier diversion.

Original languageEnglish
Pages (from-to)1209-1212
Number of pages4
JournalComparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology
Volume88
Issue number4
DOIs
Publication statusPublished - 1987

Fingerprint

Dive into the research topics of 'A glycosylated proteolipid protein is common to CNS myelin of recent lungfish (Ceratodiae, Lepidosirenidae)'. Together they form a unique fingerprint.

Cite this