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J. Biochem, 1984, Vol. 95, No. 6 1569-1575
© 1984 Japanese Biochemical Society

research-article

A Circular Dichroism Study on Thermal Denaturation of a Dimeric Globular Protein, Streptomyces Subtilisin Inhibitor1

Tomoko KOMIYAMA, Makoto MIWA, Tetsuo YATABE and Hiroshi IKEDA

Department of Industrial Chemistry, Seikei University Musashino, Tokyo 180

Thermal denaturation of Streptomyces subtilisin inhibitor was studied by means of circular dichroism (CD) measurements in the far-UV and near-UV regions. The denaturation was found to be largely reversible; the partial irreversibility was associated with a slight loss of the inhibitory activity. Difference CD spectra in the far-UV region clarified the existence of two distinct steps in the thermal transition of the secondary structure. The first step below 80°C is attributable to a partial conformational change in the a-helix portion, whereas the second step between 80°C and 94°C is attributable to a major conformational change involving the ß-sheet portion. On the assumption that the major denaturation involves dissociation of the SSI into its subunits, the enthalpy and entropy changes were determined to be 216 kcal·mol–1 and to be 603 cal·deg–1·mol–1, respectively.

1This study was supported in part by a grant, No. 536005 (1980–1982), from the Ministry of Education, Science and Culture of Japan.


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