Atkins C A, Patterson B D, Graham D
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.
Plant Physiol. 1972 Aug;50(2):218-23. doi: 10.1104/pp.50.2.218.
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.
碳酸酐酶(EC.4.2.1.1)从双子叶植物豌豆(Pisum sativum L.)的叶片中纯化得到(56倍纯化),也从单子叶植物白花紫露草(Tradescantia albiflora Kunth.)的叶片中纯化得到(24倍纯化)。豌豆酶的分子量估计为188,000 ± 8,000,亚基大小为28,000 ± 3,000和56,600 ± 3,500。每32,500 ± 2,000克蛋白质含有1摩尔锌。白花紫露草酶的分子量估计为42,000 ± 2,000,亚基大小为27,500 ± 2,200。每34,000 ± 2,000克蛋白质含有1摩尔锌。这两种酶制剂在比活性、溶液稳定性以及对磺胺类药物和无机阴离子的敏感性方面存在差异。凝胶电泳将每种纯化制剂分离成两条活性酶带。