Catalase has been isolated from toad liver in a crystalline form.
Kat.-f. of the crystal is 21600 and its crystalline form is a square thin plate.
A recrystallized crystal shows a single boundary in electrophoretic analysis, and its mobility is -2.8×10
-_??_ cm
2/V sec. at pH 7.0.
A cow liver catalase isolated at the same time has a mobility of -3.1×10
-5 cm
2/V sec. at pH 7.0.
The activity of crystalline toad liver catalase has its optimum at 15° and this
temperature is in accordance with the optimum of the extracted solution, namely, the optimum temperature is constant even when the enzymes are purified to take crystalline forms.
The same experiments were made on the cow liver catalase and we have found that the optimum temperature of the cow liver catalase was 40° upon measuring both extracted solutions and crystalline enzymes.
These results show that the optimum temperatures of catalase are differ accord-ing to the sources from which they are extracted and that this difference is to be attributed to, the . protein parts of the enzyme molecules.
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