Purification and characterization of vitellin from the estuarine mysid Neomysis integer (Crustacea; Mysidacea)

Comp Biochem Physiol A Mol Integr Physiol. 2004 Aug;138(4):427-33. doi: 10.1016/j.cbpb.2004.05.012.

Abstract

Invertebrates account for roughly 95% of all animals, yet surprisingly, little effort has been invested to understand their value in signaling potential environmental endocrine disruption. There has been, however, much recent attention on vitellogenin induction in egg-laying invertebrates and vertebrates as indicators of exposure to estrogenic xenobiotics. Mysid shrimp (Crustacea: Mysidacea) have been put forward by several researchers and regulatory bodies (e.g., US-EPA) as suitable test organisms for the evaluation of environmental endocrine disruption. In view of developing sensitive assays to study endocrine disruption in the estuarine mysid Neomysis integer, we isolated and characterized vitellin, the major yolk protein in eggs. Vitellin was purified using gel filtration and characterized by electrophoresis using different staining procedures. Specific (as shown by Western blotting) polyclonal antibodies were produced in rabbit against the purified vitellin of N. integer. These antisera will be used to develop immunoassays to study vitellogenesis in mysids and to detect potential stimulatory or inhibitory effects of endocrine disruptors on the production of vitellin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibody Specificity
  • Blotting, Western
  • Chromatography, Gel
  • Crustacea / immunology
  • Crustacea / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Immune Sera / immunology
  • Molecular Weight
  • Protein Subunits / isolation & purification
  • Protein Subunits / metabolism
  • Vitellins / chemistry
  • Vitellins / immunology
  • Vitellins / isolation & purification*
  • Vitellins / metabolism*

Substances

  • Immune Sera
  • Protein Subunits
  • Vitellins