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- W2128871425 abstract "The activity of carbon,ic anhydrase can be determined by three methods, manometric, electrometric and colorimetric. The manometric procedure (Roughton & Booth, 1938 and 1946) is considered to be the most reliable but technically difficult. Both the electrometric (Wilbur & Anderson 1948) and colorimetric (Philpot & Philpolt 1936 and Roughton & Booth 1946) methods are founded on the change of pH, when H,CO:, is farmed from CO, and H,O, implying an increase of the acidity. The enzyme activity is then calculated as the inverse value of the number of seconds required to obtain a certain of pH. It may therefore be remarked that the enzyme has to react during a continuous change of pH, which will give a continuous fall of its activity. It may also be observed that some indicators inhibit the enzyme. These disadvantages diminish the reliability of the electronic and colorimetric methods. In this paper a new modification for determination of carbonic anhydrase activity is presented. The pH of the solution is kept constant during the entire determination. A preliminary note on the method has previously been published (Holmgkd 1960). The reaction is performed in an automatic titrator. Similar methods have been described for other enzymes, for instance acetylcholinesterase. When CO, reacts to H,CO,, the appropriate quantity of NaOH for maintsnce of a constant pH is automatically and contiiiuously added." @default.
- W2128871425 created "2016-06-24" @default.
- W2128871425 creator A5032503834 @default.
- W2128871425 date "1961-01-01" @default.
- W2128871425 modified "2023-09-26" @default.
- W2128871425 title "On the Determination of Carbonic Anhydrase in Biological Material" @default.
- W2128871425 cites W1487680459 @default.
- W2128871425 cites W1894513809 @default.
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- W2128871425 doi "https://doi.org/10.1080/00365516109137304" @default.
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