Abstract
An alkaline inorganic pyrophosphatase (E.C. 3.6.1.1) has been detected in a range of species and is associated at least partly with the chloroplast fraction. It is as active in plants showing only the carbon reduction cycle of carbon dioxide fixation as in plants exhibiting the 4-carbon acid pathway. The enzyme has been isolated and partially purified from sugar cane leaves. It has an absolute requirement for magnesium ions and shows a pH optimum of 8·3. It is inhibited by orthophosphate, arsenate and EDTA but is unaffected by -SH group inhibitors. Possible functions of the pyrophosphatase are discussed.
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