Abstract
Carbonic anhydrase (CA) was purified to homogeneity from maize leaves, and antibodies to the purified protein raised using rabbits. Western blot analyses using antibodies to the purified maize leaf CA indicated cross-reactivity with leaf extracts from a variety of C3 and C4 monocotyledonous and dicotyledonous plants. However maize leaf CA antibodies quantitatively titrated CA activity only in leaf extracts of maize and sorghum. Pretitration of crude leaf extracts with maize CA antibodies and activity measurements, together with Western blot analyses of the resultant samples, indicated that there are isozymic forms of CA in plant leaf tissues in both C3 and C4 plants which are similar in size but which differ antigenically from the maize leaf CA.
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