Abstract
A micromodification of the classical Meldrum and Roughton manometric method for determining carbonic anhydrase activity is presented. The method is sensitive enough to measure carbonic anhydrase activity in a single rat thyroid gland or in 0.01 μl of blood. The effect of various homogenization media (isotonic sucrose, isotonic NaCl, and H 2O) on the recoverable carbonic anhydrase activity illustrates a disadvantage in the use of an electrolyte medium. In the NaCl medium, approximately one-third of the total activity recoverable from isotonic sucrose or H 2O medium is lost to the readily sedimented fraction of the homogenate. The activity in the sedimented fraction appears to be associated with clumped mitochondria. Enzymic activity is expressed in arbitrary units calculated from the reaction time. All units are derived from a common reaction time interpolated from concentration-activity curves. The expression of enzymic activity in such a manner yields units which are directly comparable. In addition, a conversion factor is calculated to permit the expression of the arbitrary units into absolute enzyme units.
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