Purification and characterization of antifreeze proteins from larvae of the beetle Dendroides canadensis
| Autor: | John G. Duman, Ding Wen Wu, Francis J. Castellino, Chi Hing C. Cheng |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
chemistry.chemical_classification
Larva Physiology Ph optimum digestive oral and skin physiology Circular dichroism spectra Biochemistry digestive system diseases Amino acid Endocrinology chemistry Antifreeze protein embryonic structures Animal Science and Zoology Random structure Dendroides canadensis neoplasms Ecology Evolution Behavior and Systematics Cysteine |
| Zdroj: | Journal of Comparative Physiology B. 161:271-278 |
| ISSN: | 1432-136X 0174-1578 |
| DOI: | 10.1007/bf00262308 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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