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. 1972 Aug;50(2):218–223. doi: 10.1104/pp.50.2.218

Plant Carbonic Anhydrases

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

C A Atkins a,1,2, B D Patterson a,3, D Graham a
PMCID: PMC366113  PMID: 16658145

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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