Extreme thermostability of tarantula hemocyanin.
- Sterner R Dept. of Biophysical Chemistry, University of Basel, Switzerland.
- Vogl T
- Hinz HJ
- Penz F
- Hoff R
- Föll R
- Decker H
- 1995-05-01
Published in:
- FEBS letters. - 1995
Adaptation, Physiological
Allosteric Regulation
Animals
Calorimetry, Differential Scanning
Cations, Divalent
Hemocyanins
Hot Temperature
Hydrogen-Ion Concentration
Light
Oxygen
Protein Conformation
Protein Denaturation
Scattering, Radiation
Spiders
Structure-Activity Relationship
English
Biotops with extreme temperatures such as deserts force animals to avoid or escape high temperatures by biochemical, behavioural or morphological adaptation. In this context we tested the resistance to heat of the oxygen carrier hemocyanin from the ancient tarantula Eurypelma californicum, which is found in arid zones of North America. Differential scanning calorimetry, light scattering, crossed immunogelelectrophoresis and oxygen binding experiments show that the 24-meric hemocyanin is conformationally stable and fully functioning at temperatures up to 90 degrees C. Our results demonstrate that the cation-mediated state of oligomerization is not only crucial for the high cooperativity of oxygen binding of this hemocyanin, but also for its extreme stability in the physiological temperature and pH range.
- Language
-
- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1016/0014-5793(95)00341-6
- PMID 7750550
- Persistent URL
- https://sonar.ch/global/documents/97314
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