Premium
Reversible thermal transition of brain myelin proteolipid
Author(s) -
Mateo P.L.,
Lopez-Lacomba J.L.,
Moreno M.C.,
de Cozar M.,
Cortijo M.,
Monreal J.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80330-1
Subject(s) - cooperativity , differential scanning calorimetry , enthalpy , chemistry , calorimetry , membrane , myelin , crystallography , transition (genetics) , biophysics , thermodynamics , biochemistry , biology , physics , neuroscience , gene , central nervous system
Brain myelin proteolipid has been investigated using high‐sensitivity differential scanning calorimetry (DSC) under various conditions. Crude proteolipid with a 40% ( ) content of protein gave rise to a reversible transition, centered at about 60°C. The specific enthalpy of the transition was 50 + 5 J·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°C.