Abstract
In contrast to other globular proteins, bovine globin forms a gel at low concentrations. Although this property is of practical importance, there have been no studies on the gelation mechanism of globin. The structural properties of globin solutions were studied by fluorescence measurement, circular dichroism (CD) and ultracentrifugal analysis and the heat-induced gelation was investigated by dynamic viscoelasticity measurements. At low pH (<5.0) both the rate constant of gelation and G′ inf were lower than at high pH values. CD and fluorescence analysis suggest that globin is more unfolded and more flexible at low pH values. When G′ was measured as a function of temperature, two peaks were observed suggesting that two different kinds of network structures are formed: a less ordered random structure above 60°C and a more ordered structure above 85°C. The former is typical for high pH gels (pH 5.7) and the latter for low pH gels (pH 4.7).
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