The method has been developed for obtaining two purified forms of carbonic anhydrase (CA, A and B forms) from amaranth (Amaranthus cruentus L.) leaves. The method includes precipitation with ammonium sulfate, fractionation by ion-exchange chromatography on DEAE Sephadex A-50, gel filtration on AcA-34 ultragel, and ion-exchange chromatography on DEAE cellulose. The molecular weights of A and B forms were different and equaled to 151 and 251 kD, respectively. The results suggest that SH groups and zinc play important roles in the catalytic activity of both CA forms. Both forms exhibited a high hydratase activity and did not represent allosteric enzymes. However, the catalytic properties of A form, evaluated from the pH dependence of kinetic parameters, differed from those of B form, which was apparently caused by dissimilar structures of these forms. Furthermore, the A form was localized in chloroplast membranes of bundle sheath cells, whereas B form was a soluble enzyme located in the cytoplasm of mesophyll cells.
Russian Journal of Plant Physiology – Springer Journals
Published: Oct 17, 2004
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