Purification and partial characterization of an ice nucleator protein from the intertidal gastropod, Melampus bidentatus

Dana L. Madison, Mona M. Scrofano, Robert C. Ireland, Stephen H. Loomis

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

An ice nucleator protein has been purified from the intertidal gastropod Melampus bidentatus by a combination of gel filtration and ion exchange chromatography. Partial characterization of this ice nucleator protein indicates that in the native form, it exists as an aggregate with a molecular weight in excess of 600 kDa. SDS-PAGE analysis indicates that this aggregate is composed of two low molecular weight protein species of approximately 16.6 and 17.4 kDa. Biochemical analysis indicates that it is neither a lipoprotein nor a glycoprotein. The amino acid composition indicates that it contains a high percentage of polar amino acids with Asx and Glx representing over 20 mol% of the protein. The characteristics of this molluskan ice nucleator protein are compared with those of purified ice nucleator proteins obtained from bacteria and various species of insects.

Original languageEnglish (US)
Pages (from-to)483-490
Number of pages8
JournalCryobiology
Volume28
Issue number5
DOIs
StatePublished - Oct 1991

    Fingerprint

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

Cite this