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. 1989 Sep;91(1):34–38. doi: 10.1104/pp.91.1.34

Purification of an H+-Translocating Inorganic Pyrophosphatase from Vacuole Membranes of Red Beet 1

Vahé Sarafian 1, Ronald J Poole 1
PMCID: PMC1061948  PMID: 16667022

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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Selected References

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