โ Scribed by Shusuke Hirano; Hiroaki Asou; Yukifumi Noda; Iekado Shibata
No coin nor oath required. For personal study only.
Preliminary experiments with a newly developed radioassay for carbonic anhydrase activity were performed. The velocity of 14COt formation from sodium [Wlbicarbonate was determined at both the nonenzymatic and enzymatic stages, and the net "CO, formation from the labeled substrate by carbonic anhydrase was calculated from the difference between these velocities. The enzyme activity could be calculated from this net CO1 formation and the r4C specific activity of the substrate. A trial using rat blood homogenates as enzyme samples revealed that the new radioassay could precisely determine the activity of carbonic anhydrase even at the dilution of 1:2000.
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