Plant Carbonic Anhydrases | Zendy

C. A. Atkins | Zendy; Brian D. Patterson | Zendy; D. Graham | Zendy

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Plant Carbonic Anhydrases

Author(s) -

C. A. Atkins,

Brian D. Patterson,

D. Graham

Publication year - 1972

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.50.2.218

Subject(s) - pisum , carbonic anhydrase , enzyme , tradescantia , sativum , biology , protein subunit , biochemistry , polyacrylamide gel electrophoresis , zinc , mole , enzyme assay , electrophoresis , specific activity , botany , chromatography , chemistry , organic chemistry , gene

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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