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Abstract:
Lipoprotein crystals of hagfish yolk platelets (Myxine glutinosa L.) are, by electron diffraction of embedded specimens, monoclinic (a > 19.8 nm, b > 8.9 nm, c > 9.0 nm, β ~ 105°; space group C2: 2 dimers per cell). Using sodium dodecyl sulfate/polyacrylamide gel electrophoresis, the four major protein bands in Myxine (molecular weights 30,000; 44,000: 80,000 and 130,000) correspond, with small differences, to similar bands of Xenopus yolk lipoproteins. The symmetric lipovitellin-phosvitin dimer in cyclostomes is unique and probably reflects the lack of diversification of homologous vertebrate protein species.
