Purification and characterization of a putative vitellogenin from the ovary of amphioxus (Branchiostoma belcheri tsingtaunese).

@article{Sun2001PurificationAC,
  title={Purification and characterization of a putative vitellogenin from the ovary of amphioxus (Branchiostoma belcheri tsingtaunese).},
  author={Xiangrong Sun and Shun-hua Zhang},
  journal={Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
  year={2001},
  volume={129 1},
  pages={121-7}
}
An oocyte-yolk protein was purified by double-step chromatography from amphioxus ovaries. The purified protein appeared to exist as a homodimer of approximately 320 kDa in native polyacrylamide gel electrophoresis (PAGE), and was reduced to a single monomer of approximately 160 kDa in sodium dodecyl sulfate-PAGE (SDS-PAGE). The protein was characterized as a phospholipoglycoprotein by native PAGE and staining of gels for phosphorus with methyl green, for lipids with oil red O and Sudan black B… CONTINUE READING