Journal of comparative physiology

, Volume 142, Issue 4, pp 539–542 | Cite as

Purification and composition of a thermal hysteresis producing protein from the milkweed bug,Oncopeltus fasciatus

  • Jean L. Patterson
  • Thomas J. Kelly
  • John G. Duman
Article

Summary

A protein which produces a thermal hysteresis (a difference between the freezing and melting points) was purified from the hemolymph of the milkweed bug,Oncopeltus fasciatus. The amino acid composition of theOncopeltus thermal hysteresis protein is somewhat different from that of the larvae of the beetle,Tenebrio molitor, which is the only other insect from which such a protein has as yet been purified. The major difference between the two is the large amount of serine (30.5% of the amino acid residues) and glycine (20.0%) present in theO. fasciatus protein. Both insect proteins have a composition which consists of approximately 60% polar amino acids and lacks large amounts of alanine. In these respects they are quite different from the fish protein antifreezes. The apparent differences in structure of the thermal hysteresis proteins and glycoproteins indicates that these proteins have evolved independently and therefore offer an interesting example of convergent evolution.

Keywords

Glycine Melting Point Serine Acid Composition Alanine 

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Copyright information

© Springer-Verlag 1981

Authors and Affiliations

  • Jean L. Patterson
    • 1
  • Thomas J. Kelly
    • 1
  • John G. Duman
    • 1
  1. 1.Department of BiologyUniversity of Notre DameNotre DameUSA

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