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

Jean L. Patterson, Thomas J. Kelly, John G. Duman

    Research output: Contribution to journalArticlepeer-review

    25 Scopus citations

    Abstract

    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 the Oncopeltus 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 the O. 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.

    Original languageEnglish (US)
    Pages (from-to)539-542
    Number of pages4
    JournalJournal of Comparative Physiology ■ B
    Volume142
    Issue number4
    DOIs
    StatePublished - Dec 1 1981

    ASJC Scopus subject areas

    • Ecology, Evolution, Behavior and Systematics
    • Biochemistry
    • Physiology
    • Animal Science and Zoology
    • Endocrinology

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