Reversible thermal transition of brain myelin proteolipid
| Autor: | María Carmen Bellver Moreno, Pedro L. Mateo, Manuel Cortijo, M. de Cozar, J. Monreal, Jose L. Lopez-Lacomba |
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| Rok vydání: | 1986 |
| Předmět: |
Protein Conformation
Thermal transition Membrane lipids Enthalpy Biophysics Cooperativity Biochemistry Differential scanning calorimetry Protein structure Structural Biology Genetics Animals Myelin Proteolipid Protein Molecular Biology Myelin proteolipid Brain Chemistry Calorimetry Differential Scanning Chemistry digestive oral and skin physiology Cell Biology Myelin Basic protein Proteolipid DSC Enthalpy Reversible thermal transition Myelin proteolipid protein Crystallography Thermodynamics Cattle lipids (amino acids peptides and proteins) Myelin Proteins |
| Zdroj: | FEBS Letters. 197:221-224 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(86)80330-1 |
| Popis: | Brain myelin proteolipid has been investigated using high-sensitivity differential scanning calorimetry (DSC) under various conditions. Crude proteolipid with a 40% (w/w) content of protein gave rise to a reversible transition, centered at about 60 degrees C. The specific enthalpy of the transition was 50 +/- 5 J X g-1 with a calorimetric to van't Hoff enthalpy ratio of 5.7 +/- 0.5. To our knowledge this is the first intrinsic membrane protein in which a reversible thermal transition has been detected and investigated by DSC. Similar experiments were carried out using the recombinants of delipidated proteolipid and the pool of natural membrane lipids; in this case the transition was less enthalpic and showed lower cooperativity. The recombinants with lecithins, however, did not show any transition at 60 degrees C. |
| Databáze: | OpenAIRE |
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