Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis

Ding W. Wu, John G. Duman, Chi Hing C. Cheng, Francis J. Castellino

Research output: Contribution to journalArticle

Abstract

Four antifreeze proteins (AFPs) were purified from larvae of the beetle Dendroides canadensis. The AFPs are similar in amino acid compositions, having high contents of hydrophilic amino acids (45-55 mol%) and cysteine (∼16 mol% Cys). Approximately half of the Cys residues form disulfide bridges, and both the disulfide bridges and free sulfhydryls are essential for activity. The N-terminals of the AFPs are blocked. The pH optimum of the AFPs is ∼7.8, but major loss of activity occurred only at very high pH (12.0). The detergents SDS and Triton X-100 did not inactivate the AFPs. Circular dichroism spectra indicate the presence of both α and β secondary structures in the AFPs, in addition to a large random structure component.

Original languageEnglish (US)
Pages (from-to)271-278
Number of pages8
JournalJournal of Comparative Physiology B
Volume161
Issue number3
DOIs
StatePublished - Jul 1 1991

Keywords

  • Antifreeze proteins
  • Beetle Dendroides
  • Insect cold tolerance
  • Thermal hysteresis proteins

ASJC Scopus subject areas

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

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