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
Catalogue details

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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    containing 4, 8, 12, 24, and 40 mgrm. dissolved in 10 cm.^ of water, which, after standing for half to one hour, were introduced in portions of 1 cm.® into five series of test-tuhes containing 286 mgrm. of salicin and 4, 9, 14, 29, and 49 cm.® respectively of water. After 15 hours’ incubation in baths at known temperatures the action was stopped and the quantity of salicin hydrolysed in each tube estimated as before. The numbers obtained are given in Table IV. Table IV. Temperatures at the beginning and end of each experiment. Salicin hydrolysed per cent, with the following substrate concentrations M/5. M/10. M/15. M/30. M/50. O 7 -3- 7 -7 10 -8 8 -3- 9 -0 6-6 9 -6- 8 -6 — — 18-3 9 -4-10 -8 — — — 26 -0 12 -0-10 -9 — — — — 35 -5 17 -2-17 -3 — 23 -0 17 -4-17 T 10 -8 17 -5-17 -6 — — 32 -5 18 -6-18 -5 — — — 57 '5 18-9 — — — 47-0 25 -2-25 -0 — — — 63 -7 26 -4-25 -7 — — — . 75 -0 26 -5 19 -2 38 -6 60 -8 30 -0 22 -3 41 -9 58 -5 75 -3 30 -5 __ — — — 75 -8 33 -5 23 -6 44-6 62 -9 80 -7 88 -3 40 -5 — — — 68 -3 76 -7 40 -7-40 -6 — 39 -4 40 -8-40 -7 22 -4 — 55 -2 45 -0-45 -2 — — — — 66 -9 45 -5-45 -3 19 -7 35 -0 43-7 45 -5 — — — 54 -7 50 -3-50 -5 15 T — 31 -9 50 -6-50 -5 — 25 -8 — 61 T-50 -8 — — — 34 -3 51 -5-51 -2 — — — 38 -3 54 -3-54 -0 11 -2 54 -2-54 -3 — 18-4 21 -4 24-3 54 -6-55 -0 — — — — 26 -8 These numbers give graphically the curves shown in fig. 4 (p. 249). On examination tlie above curves indicate, although with very different degrees of precision, maxima in the same region of temperature. In so far as the curves are comparable with one another, they produce the general impression that the optimum temperature of the enzyme is constant, and consequently independent of the concentration of the substrate. But to answer the question more definitely curves of a uniform type, easily com-