Abstract
Viscosity measurements were made in the temperature range of 10 °–40 °C. The equationν=ν o exp(B/(T-T o )) was used with the parameterT 0 as “structure indicator”, which is called the “limiting temperature”. For instance, hydrocarbons, as liquids with “quasifree” molecules, haveT 0=O; water as a highly structured liquid hasT 0= 140–150 K. The polymer investigated was ovalbumin in aqueous solution in a concentration comparable to that of blood. Acetylsalicylic acid produces a protein conformation which breaks the water structure in solution at a pH of within the in vivo region. The question of whether only the acidity determines the water structure breaking properties of the protein is investigated by acidifying albumin-water solutions with hydrochloric acid, lysine chloride and ascorbic acid. All these acids exhibit similar effects. A stronger influence is observed for ammonium chloride. Its interaction with ovalbumin produces a strong structure-breaking effect. The most powerful water structure breaker in albumin-water solutions is dextrane. In a concentration of 10 % it changes the polymer conformation so that the water structure is broken to such an extent that the solution behaves as an almost “quasifree” liquid withT 0=O.
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