Carbonic anhydrase as a tool in studying the mechanism of reactions involving H2CO3, CO2 or HCO3−
- 1 January 1948
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 43 (4) , 550-555
- https://doi.org/10.1042/bj0430550
Abstract
[long dash]When a powerful Jack bean urease prepn. was allowed to act upon a limited quantity of urea in a neutral buffer at 15[degree]C, CO3 was rapidly evolved and later gradually reabsorbed. If ox blood carbonic anhydrase was added, no excess of CO2 was evolved. These results support the conception that CO2, and not bicarbonate or carbonate is a primary intermediate in the action of urease on urea. Carbonic anhydrase had a similar effect in the yeast carboxylase-pyruvate system under certain described conditions. The results indicated that CO2, not bicarbonate or carbonic acid is the primary product in the enzymic decarboxylation of pyruvate. The effects of adding carbonic anhydrase to systems in which CO2 or bicarbonate are reactants and the use of Warburg manometers for detn. of carbonic anhydrase activity were discussed.This publication has 3 references indexed in Scilit:
- The manometric determination of the activity of carbonic anhydrase under varied conditionsBiochemical Journal, 1946
- The direct chemical estimation of carbamino compounds of CO2with haemoglobinThe Journal of Physiology, 1934
- The state of carbon dioxide in bloodThe Journal of Physiology, 1933