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 language | English (US) |
|---|---|
| Pages (from-to) | 483-490 |
| Number of pages | 8 |
| Journal | Cryobiology |
| Volume | 28 |
| Issue number | 5 |
| DOIs | |
| State | Published - Oct 1991 |
| Externally published | Yes |
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology
- General Agricultural and Biological Sciences