Chapter

Applications of Mass Spectrometry in Life Safety

Part of the series NATO Science for Peace and Security Series A: Chemistry and Biology pp 23-36

Structure, Processing, and Polymerization of Rainbow Trout Egg Vitelline Envelope Proteins

  • Costel C. DarieAffiliated withDepartment of Molecular, Cell and Developmental Biology, Mount Sinai School of Medicine Email author 
  • , Eveline S. LitscherAffiliated withDepartment of Molecular, Cell and Developmental Biology, Mount Sinai School of Medicine
  • , Paul M. WassarmanAffiliated withDepartment of Molecular, Cell and Developmental Biology, Mount Sinai School of Medicine Email author 

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Abstract

Mammalian and non-mammalian eggs are surrounded by a zona pellucida (ZP) and vitelline envelope (VE), respectively. The rainbow trout egg VE consists of three proteins, VEα, VEβ, and VEγ, which are related to mouse egg ZP proteins ZP1, ZP2, and ZP3. Mass spectrometry (MS) has been used extensively to identify the intramolecular disulfide linkages and the cellular site of proteolytic processing of trout VE proteins. Additionally, Blue Native-PAGE (BN-PAGE) has been used to investigate polymerization of purified trout VE proteins under non-denaturing conditions. Results of these experiments reveal that, despite ~400 million years separating the appearance of trout and mice, and the change from external to internal fertilization and development, VE and ZP proteins have a great deal in common.