Thermal lability of bovine erythrocyte membrane proteins was studied by electron spin resonance using maleimide spin label. The temperature of the sample during measurements could be varied for the first time between 0 and 60 degrees C with an accuracy of +/- 0.1 degrees C. Our results show that "old" erythrocyte membrane proteins are less stable against thermal denaturation then "young" cells.

In this study the effect of the alkylating agent, sulfur mustard, on calf thymus chromatin was investigated using UV/Vis spectroscopy, gel electrophoresis and thermal denaturation techniques. The results show that treatment of isolated chromatin with sulfur mustard releases histones from the core particles but does not affect histone H I and nonhistone chromosomal proteins. The content of ...

The aim of this study was to determine the effect of pentosan polysulphate on the thermostability of alcohol dehydrogenase. Spectral analyses showed that this compound is able to increase thermostability of the enzyme and entirely eliminate thermal aggregation of YADH. These findings indicate that this heparinoid can not only modulate the enzyme activity (it has been presented in our recent pap...

Thermal processing often results in disruption of the native conformation of whey proteins, thus affecting functional properties. The aim of this work was to evaluate the effects of moderate electric fields on denaturation kinetics and thermodynamic properties of whey protein dispersions at temperatures ranging from 75 to 90 °C. Application of electric fields led to a lower denaturation of whey...

Solutions of fibrinogen show two endothermal (denaturing) transitions, at 61 degrees and at 100 degrees , when heated in a differential scanning calorimeter. Similar transitions are observed for a mixture of the fragments D and E obtained by limited proteolysis of fibrinogen. Isolated fragment E shows only a single transition, at 97 degrees . The independent thermal denaturation of these portio...

The kinetics of thermal denaturation of ceruloplasmin in water and in water with different percentage of D2O in the temperature range 25-85 degrees C, following the optical density change of the 610 nm charge transfer band of the protein has been investigated. A temperature Tt approximately equal to 65 degrees C above which an irreversible denaturation process of the protein active site takes p...

Quantifiable prognostic indicators are of considerable practical value following thermal injury. Collagen is a major component of the skin, and is known to undergo denaturation at the elevated temperatures associated with burns. The purpose of this study was to determine whether a recently developed, non-invasive imaging technique could detect and quantify collagen denaturation in burned human ...

We compared thermally induced denaturation and aggregation of two isoforms of the isolated myosin head (myosin subfragment 1, S1) containing different "essential" (or "alkali") light chains, A1 or A2. We applied differential scanning calorimetry (DSC) to investigate the domain structure of these two S1 isoforms. For this purpose, a special calorimetric approach was developed to analyze the DSC ...

The thermal denaturation and aggregation of the HbGp, in the oxy- and cyanomet-forms, was investigated by DSC, AUC, DLS, optical absorption and CD, in the pH range from 5.0 to 7.0. Oxy-HbGp has a denaturation process partially reversible and dependent on the temperature. DSC melting curve is characterized by a single peak with T(c) value of 333.4 ± 0.2K for oxy-HbGp, while two peaks with T(c) v...