STUDY OF THE HYDRATION OF PROTEINS BY THERMOGRAVIMETRY,
REDSTONE SCIENTIFIC INFORMATION CENTER REDSTONE ARSENAL ALA
Pagination or Media Count:
Thermogravimetric investigation was conducted by con tinuous or isothermal heating of various proteins treated or not treated with acetaldehyde and high polymers casein, gelatin, fibrin, edestin, bovine serum albumin, protamin, hylon, rilsan. The study of the affinity of proteins and, in general, of high polymers for water is capable of furnishing useful data on the number and arrangement of polar groups, as has been shown by Bull, Pauling and others. In addition, the dry weight of solutions of pure proteins is one of the characteristics most frequently measured with a view of determining the concentration. However, Bull has shown in his now classic paper that the dry weight of a protein is far from being independent of the temperature and duration of heating. By studying the weights of proteins after maintaining them for two hours at different temperatures between 80 and 137 degrees, this author arrives at thee conclusion that there is no temperature at which a constant weight may be obtained. This statement is not entirely justified, since a kinetic study of the weight at different temperatures does not seem to have been carried out. The thermobalance is the instrument of choice for such a study, since it makes it possible to carry out weight recordings at constant temperatures of long duration.