Structure, processing, and polymerization of rainbow trout egg vitelline envelope proteins

Costel C. Darie, Eveline S. Litscher, Paul M. Wassarman

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

1 Scopus citations


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.

Original languageEnglish
Title of host publicationApplications of Mass Spectrometry in Life Safety
EditorsCrisan Popescu, Alina Zamfir, Nicolae Dinca
Number of pages14
StatePublished - 2008

Publication series

NameNATO Science for Peace and Security Series A: Chemistry and Biology
ISSN (Print)1874-6489


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