Purification of an H+-Translocating Inorganic Pyrophosphatase from Vacuole Membranes of Red Beet
- 1 September 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 91 (1), 34-38
- https://doi.org/10.1104/pp.91.1.34
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.This publication has 17 references indexed in Scilit:
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