The optimum temperature of salicin hydrolysis by enzyme action is independent of the concentrations of substrate and enzyme / by Arthur Compton ; [communicated by Sir J.R. Bradford].

  • Compton, Arthur.
Date:
1914
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Licence: In copyright

Credit: The optimum temperature of salicin hydrolysis by enzyme action is independent of the concentrations of substrate and enzyme / by Arthur Compton ; [communicated by Sir J.R. Bradford]. Source: Wellcome Collection.

Provider: This material has been provided by The Royal College of Surgeons of England. The original may be consulted at The Royal College of Surgeons of England.

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    the optimum temperature determined in actions of 15 hours’ duration with quantities of the enzymic specimen giving concentrations varying between 1'8 X IQ-''’ and 18 x 10“^ grm. per cm.^. The numbers obtained are given in Table VI. The results are recorded graphically in fig. 10. The curves of fig. 10, as well as the M/30 curve of fig. 4 and that of fig. 8, show that the optimum temperature of the enzyme is the same in each, and, consequently, independent of the concentration of the enzyme. This holds true, as shown by two of the curves in fig. 10, even when the proportion of enzyme to substrate is more than sufficient to produce complete hydrolysis of the substrate at the optimum point. Here the optimum point is imaginary, and corresponds to the intersection of the curves representing respectively the activation and the destruction of the enzyme by heat. Briefly, then, the outcome of the inquiry is, for an action of known duration, the optimum temperature of the enzyme investigated is independent alike of the concentration of the substrate and of the concentration of the enzyme. Whether the statement be true of enzymes in general—as theoretical con- siderations would lead one to expect—I propose to answer by fresh experiments on other types of enzymes. Haeeison and Sons, Printers in Ordinary to His Majesty, St. Martin’s Lane.
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