Volumetric characterization of the thermal denaturation of α-chymotrypsin at pH 2.2
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KINETIC STUDY OF THE pH INFLUENCE ON BSA THERMAL DENATURATION
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thermal denaturation of α-amylase from bacillus amyloliquefaciens in the presence of sodium dodecyl sulphate*
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Characterization of the thermal denaturation of Bence-Jones proteins by ultracentrifugation at elevated temperatures.
The unusual thermosolubility properties of BenceJones 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 difIerences in their ultracentrifugal properties at high...
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ژورنال
عنوان ژورنال: The Journal of Chemical Thermodynamics
سال: 2020
ISSN: 0021-9614
DOI: 10.1016/j.jct.2020.106147