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

Conference paper

DOI: 10.1007/978-1-4020-8811-7_2

Part of the NATO Science for Peace and Security Series A: Chemistry and Biology book series (NAPSA)
Cite this paper as:
Darie C.C., Litscher E.S., Wassarman P.M. (2008) Structure, Processing, and Polymerization of Rainbow Trout Egg Vitelline Envelope Proteins. In: Popescu C., Zamfir A.D., Dinca N. (eds) Applications of Mass Spectrometry in Life Safety. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht

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.

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Copyright information

© Springer Science + Business Media B.V 2008

Authors and Affiliations

  1. 1.Department of Molecular, Cell and Developmental BiologyMount Sinai School of MedicineNew York10029-6574
  2. 2.Department of Structural Biology, Skirball Institute of Biomolecular MedicineNew York UniversityNew York

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