Purification of an h-translocating inorganic pyrophosphatase from vacuole membranes of red beet |
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Authors: | Sarafian V Poole R J |
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Affiliation: | Department of Biology, McGill University, Montréal, P.Q., Canada H3A 1B1. |
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Abstract: | An H+-translocating inorganic pyrophosphatase (PPase) was isolated and purified from red beet (Beta vulgaris L.) tonoplast. One major polypeptide of molecular weight 67 kilodalton copurified with fluoride-inhibitable PPase activity when subjected to one-dimensional polyacrylamide gel electrophoresis. Overall, a 150-fold purification of the PPase was obtained, from the tonoplast fraction, through anion exchange chromatography of the detergent-solubilized membranes followed by ammonium sulfate precipitation and gel filtration chromatography. The purified polypeptide showed no cross-reactivity with antibodies raised against the 67 kilodalton subunit of the tonoplast ATPase. |
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