Penguin egg‐white and polar fish blood‐serum proteins
The development of, and findings in, a long‐term research program on penguin proteins and polar fish blood proteins are described. Two of the egg‐white proteins from the Adelie penguin ( Pygoscelis adeliae ) have unique properties: a glycoprotein named penalbumin that is a major constituent with som...
| Published in: | International Journal of Peptide and Protein Research |
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| Main Author: | |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1982
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| Online Access: | http://dx.doi.org/10.1111/j.1399-3011.1982.tb03030.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1399-3011.1982.tb03030.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1982.tb03030.x |
| Summary: | The development of, and findings in, a long‐term research program on penguin proteins and polar fish blood proteins are described. Two of the egg‐white proteins from the Adelie penguin ( Pygoscelis adeliae ) have unique properties: a glycoprotein named penalbumin that is a major constituent with some characteristics similar to ovalbumin, and an ovomucoid with strong inhibitory capacity for subtilisin as well as for bovine trypsin and α‐chymotrypsin. The antifreeze glycoproteins from Antarctic fish ( Trematomus borchgrevinki and Dissostichus mawsoni ) and an Arctic fish ( Boreogadus saida ) appear to function noncolligatively by lowering the freezing temperature without affecting the melting point. Current evidence indicates that the antifreeze glycoprotein functions at the ice‐solution interface, either on the ice surface or in a transition layer between the solution and the ice. |
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