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A pH-rate determination of the activity-pH profile of enzymes. Application to yeast pyruvate decarboxylase demonstrating the existence of multiple ionizable groups

✍ Scribed by Frank Jordan; Donald J. Kuo; Ernst U. Monse


Publisher
Elsevier Science
Year
1978
Tongue
English
Weight
271 KB
Volume
86
Category
Article
ISSN
0003-2697

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✦ Synopsis


A pH-rate method, based on following the time dependence of hydroxide release by monitoring the pH drift as a function of time, is developed and applied to the construction of a detailed log activity vs pH profile for yeast pyruvate decarboxylase. In the pH range of 5 to 7 at 30°C this method reproduces the results of conventional initial rate studies but, in addition, produces a hitherto unreported pH independent activity region between pH 5.4-5.8. At least four pKs can be discerned in the pH-activity profile of this enzyme, instead of the two previously reported.