Journal of Protein Chemistry

, Volume 7, Issue 6, pp 667–687 | Cite as

Egg-white and blood-serum proteins functioning by noncovalent interactions: Studies by chemical modification and comparative biochemistry

  • Robert E. Feeney
  • David T. Osuga
Invited Contribution—Introspections On A 75th Birthday

Abstract

Some of the more interesting and important proteins are those that function by forming associations or complexes with other substances. The structure-function relationships of three of these with very different substances are transferrins, which chelate metal ions; avian ovomucoids, which form complexes with proteolytic enzymes; and antifreeze glycoproteins, which interact at the ice-solution interface. Interrelating studies on the comparative biochemistry with studies using chemical modification have helped identify the side-chain groups of the proteins involved in function as well as to be useful for studies on general protein chemistry. The most strongly associated interaction is the chelation of iron by transferrin, with an association constant of ∼1021; tyrosines, histidines, and sometimes aspartate are involved. For ovomucoids, individual substratelike residues such as lysine are involved in a Michaelis-like complex, and association constants are as high as 1010. By contrast, the antifreeze glycoproteins appear to function by a polymeric interaction at the surface of ice, wiht a much weaker association.

Key words

antifreeze glycoproteins ovomucoids transferrins comparative biochemistry protein modification 

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Copyright information

© Plenum Publishing Corporation 1988

Authors and Affiliations

  • Robert E. Feeney
    • 1
  • David T. Osuga
    • 1
  1. 1.Department of Food Science and TechnologyUniversity of CaliforniaDavis

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