Structure and properties of ovalbumin

J Chromatogr B Biomed Sci Appl. 2001 May 25;756(1-2):189-98. doi: 10.1016/s0378-4347(01)00108-6.

Abstract

Ovalbumin is a protein of unknown function found in large quantities in avian egg-white. Surprisingly, ovalbumin belongs to the serpin family although it lacks any protease inhibitory activity. We review here what is known about the amino acid sequence, post-translational modifications and tertiary structure of ovalbumin. The properties of ovalbumin are discussed in relation to their possible functional significance. These include reasons for failure of ovalbumin to undergo a typical serpin conformational change involving the reactive centre loop, which explains why ovalbumin is not a protease inhibitor, and also the natural conversion of ovalbumin to the more stable "S" form.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Models, Molecular
  • Ovalbumin / chemistry*
  • Ovalbumin / metabolism*
  • Protein Processing, Post-Translational
  • Serpins / chemistry
  • Serpins / metabolism
  • Structure-Activity Relationship

Substances

  • Serpins
  • Ovalbumin