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Plant Carbonic Anhydrases

II. Preparation and Some Properties of Monocotyledon and Dicotyledon Enzyme Types

^a Plant Physiology Unit, Commonwealth Scientific and Industrial Research Organization, Division of Food Research, and School of Biological Sciences, Macquarie University, North Ryde, 2113, Sydney, Australia

Carbonic anhydrase (EC.4.2.1.1) was purified from leaves of the dicotyledon Pisum sativum L. (56-fold) and from leaves of the monocotyledon Tradescantia albiflora Kunth. (24-fold). The molecular weight of the Pisum enzyme was estimated to be 188,000 ± 8,000 with subunit sizes of 28,000 ± 3,000 and 56,600 ± 3,500. It contained 1 mole zinc per 32,500 ± 2,000 g protein. The molecular weight of the Tradescantia enzyme was estimated to be 42,000 ± 2,000 with a subunit size of 27,500 ± 2,200. It contained 1 mole zinc per 34,000 ± 2,000 g protein. The two enzyme preparations were different in specific activity, stability in solution, and sensitivity to sulfonamides and inorganic anions. Gel electrophoresis separated each purified preparation into two active enzyme bands.

² Present address: c/o International Atomic Energy Agency, P.O. Box 645, A-1011 Vienna, Austria.

³ Present address: East Malling Research Station, East Malling, Maidstone, Kent, U.K.

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