Characterization of the Thermal Denaturation of Bence-Jones Proteins by Ultracentrifugation at Elevated Temperatures
Kenneth E. Neet 1 and Frank W. Putnam 1
From the
1 From the Department of Biochemistry, College of Medicine, University of Florida, Gainesville, Florida 32603
The unusual thermosolubility properties of Bence-Jones proteins have been investigated by the technique of ultracentrifugation at elevated temperature. Study of several purified Bence-Jones proteins has allowed description of the molecular changes that occur upon heating. Although the proteins participate in a common phenomenon, individual differences in their ultracentrifugal properties at high temperatures were observed. In certain cases an initial polymerization, followed by a depolymerization to an unfolded molecule, occurred as the temperature was raised. Sulfhydryl-binding reagents had little effect on the high temperature reactions, whereas ethanol, urea, detergents, or salts had a large effect. Therefore, the precipitation and redissolution phenomenon is attributed to alterations in the noncovalent bonding and tertiary structure of the Bence-Jones protein.
Submitted on August 9, 1965
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