[Multiplicity of molecular forms and thermostability of Torula thermophila UzPT-1 protease].
Alkaline protease preparations with different ratio of molecular forms are isolated from cultural medium of thermophilic fungi Torula thermophila UzPT-1 by means of protein fractionation with (NJ/)2SO4 and gel filtration through Sephadex G-75. The enzyme preparations differ in their thermostability in water at 60 degrees C. High molecular weight oligomeric enzyme forms dissociate in water (at 2-4 degrees C) forming dimeric and monomeric forms. Disaggregation is accompanied by the change in the thermostability of the enzyme preparations. It is concluded that protease thermostability depends on the ratio of dimeric and monomeric forms of the preparation, and it is associated with the conformational state of the enzyme molecules, and it is associated with the conformational state of the enzyme molecules. Oligomeric forms do not dissociate in 1% sodium dodecylsulphate and in 6 M urea. Ca2+ produces dissociation of high molecular weight enzyme forms and the conformational transition into the thermostable state.
D055598:Chemical Phenomena; D002621:Chemistry; D003454:Cryptococcus / Q000201:enzymology*; D004355:Drug Stability; D006358:Hot Temperature; D046911:Macromolecular Substances; D008970:Molecular Weight; D010447:Peptide Hydrolases; D011487:Protein Conformation
D046911:Macromolecular Substances; D010447:Peptide Hydrolases
Mnozhestvennost' molekuliarnykh form i termostabil'nost' proteazy griba Torula thermophila shtamm uzPT-1