[Two forms of carbonic anhydrase from bean chloroplasts].
The intracellular localization of carboanhydrase from the bean (Vicia faba) leaves was investigated. The bulk of the enzyme activity (about 70%) is localized in the chloroplasts. The enzyme exists both in the soluble and in membrane-bound state. Disc electrophoresis in polyacrylamide gel with specific staining for the enzyme activity demonstrated that the soluble and membrane-bound carboanhydrases from bean chloroplasts are two molecular forms (presumably isoenzymes) differing in their electrophoretic mobilities. Protein fractionation with (NH4)2SO4 and a subsequent gel filtration on Sephadex G-200 and isoelectrofocusing resulted in separation of the two forms and their purification to homogeneity. Both carboanhydrases differ in pH, specific activity and stability.
D002256:Carbonic Anhydrases / Q000302:isolation & purification*; D002736:Chloroplasts / Q000201:enzymology*; D007887:Fabaceae / Q000201:enzymology*; D007425:Intracellular Membranes / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification*; D008970:Molecular Weight; D010946:Plants, Medicinal
D007527:Isoenzymes; D002256:Carbonic Anhydrases
Dve formy karboangidrazy v khloroplastakh bobov.