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Updated: Jun 19, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO
J M Nelson1, E T Palmer, B G Wilkes
1Department of Chemistry, Columbia University, New York.
Abstract:
1. A method is given whereby the course of hydrolysis of sucrose by live yeast cells may be followed with precision equal to that found when invertase solutions prepared from autolyzed yeast are used to cause inversion. 2. The practical value of the equation of Nelson and Hitchcock as a means of following the course of enzymic hydrolysis of sucrose is hereby extended. 3. The inversion of sucrose by live yeast cells and by extracted invertase has been quantitatively compared. 4. The course of hydrolysis of sucrose by the invertase of Fleischmann's yeast has been found to be identical in vivo and in vitro.
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