Thermal denaturation of streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex.
Thermal denaturation of streptomyces subtilisin inhibitor, subtilisin BPN', and the inhibitor-subtilisin complex.
复制标题
链霉菌枯草杆菌蛋白酶抑制剂、枯草杆菌蛋白酶 BPN 和抑制剂-枯草杆菌蛋白酶复合物的热变性。
DOI：
10.1021/bi00524a042
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发表时间：
1981
期刊：
影响因子：
2.9
通讯作者：
Sturtevant,JM
中科院分区：
文献类型：
--
作者：
Takahashi,K;Sturtevant,JM
Katsutada Takahashi** and Julian M. Sturtevant* abstract: The thermal unfolding of the microbial proteinase inhibitor Streptomyces subtilisin inhibitor (SSI)[Sato, S., & Murao, S.(1973) Agrie. Biol. Chem. 37, 1067-1074), the bacterial proteinase subtilisin BPN'(EC 3.4. 21.14), and the complex formed bythese twoproteins has been studied by differential scanning calorimetry (DSC). The thermal de-naturation of SSI at pH 7.00 is fully reversible while those of subtilisin BPN'and its complex with SSI are not. The DSC data show that dimeric SSI remains dimeric as the temperature is raised until it unfolds and that it then dissociates during the unfolding process. The apparent specific heat of denaturedStreptomyces subtilisininhibitor (SSI), isolated from Streptomyces albogriseolus, strongly inhibits bacterial proteinases such as subtilisin BPN', with inhibition constants as high as 1010 M. The inhibitor consists of two identical sub-units, each containing a polypeptide chain of 113 amino acid residues with 2 intrachain disulfide bridges. Each subunit, of molecular weight 11483, binds to one molecule of subtilisin to form a complex E2I2 (Inouye et al., 1978). The amino acid sequence of the inhibitor was determined by Ikenaka et al.(1974), and its three-dimensional structure has been recently
