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M Petec

Publications and source records attributed to M Petec.

15 recordsLinked to original sources

The thermal transition of brain soluble proteins.

Soluble rat brain proteins undergo a thermal reversible denaturation in the range of 20 degrees C -65 degrees C. The thermal transition as studied in 0.25 M sucrose solution, is associated with changes in the proteins ionization capacity by the lowering of the isoionic solution pHfrom a value of 6.95 at 20 degrees C to 6.55 at 65 degrees C. The apparent enthalpy change delta H at the transition temperature (t=50 degrees C) is about 34 Kcal, heat capacity delta Cp about 1.75 Kcal, and apparent entrophy change deltaS 100 e.u. The data suggest that the thermal transition is predominantly a two-state process. A prolonged keeping of the protein solution at the increased temperature produces a partial reversibility of thermal transitions by a lowering of 5-HT cations fixing on the protein molecule.

Animals

Relationship between bovine serum albumin structure and its chemical equilibria with hydrogen and 5-hydroxytryptamine ions.

From the analysis of titration curves with hydrogen and 5-HT ions, it was found that the electrostatic interaction parameter of protein macroion and the number sites of 5-HT fixing were smaller over an acid and base pH range as compared to their values at neutral pH. Our data were interpreted by the conformational changes which can be induced when BSA is exposed to denaturation by acid and alkali pH.

Animals