The Effects of Polyhydric and Monohydric Alcohols on the Heat Induced Reversible Denaturation of Chymotrypsinogen A
この論文をさがす
説明
<jats:p>The reversible thermal denaturation of chymotrypsinogen A was investigated in aqueous solutions of mono‐, di‐ and polyvalent alcohols.</jats:p><jats:p>Sorbitol and erythritol show a stabilizing effect, whereas the di‐ and monovalent alcohols are destabilizing. Divalent alcohols have a less destabilizing influence than monovalent alcohols when equimolecular proportions of ‐CH<jats:sub>2‐</jats:sub> and / or –CH<jats:sub>3</jats:sub> groups are present.</jats:p><jats:p>Stabilizing effects of the polyalchols can be explained in terms of a lessened H bond rupturing capacity of the medium.</jats:p><jats:p>The destabilizing by di‐ and movovalent alcohols is attributed to their hydrophobic interaction with the protein, which increases with the number of ‐CH<jats:sub>2‐</jats:sub> and, or ‐CH<jats:sub>3</jats:sub> groups and decreases with the number of ‐OH groups.</jats:p><jats:p>Chymotrypsinogen A is more destabilized by hydrophobic alcohols than ribonuclease.</jats:p>
収録刊行物
-
- European Journal of Biochemistry
-
European Journal of Biochemistry 14 (1), 150-153, 1970-05
Wiley