A symmetric lipovitellin-phosvitin dimer in cyclostome yolk platelet crystals: 
structural and biochemical observations

Lange, Rainer H.; Richter, Hans-Peter

doi:10.1016/0022-2836(81)90188-1

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A symmetric lipovitellin-phosvitin dimer in cyclostome yolk platelet crystals: structural and biochemical observations

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Richter, Hans-Peter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Lange, R. H., & Richter, H.-P. (1981). A symmetric lipovitellin-phosvitin dimer in cyclostome yolk platelet crystals: structural and biochemical observations. Journal of Molecular Biology (London), 148(4), 487-491. doi:10.1016/0022-2836(81)90188-1.

Cite as: https://hdl.handle.net/21.11116/0000-0008-277E-0

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.