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- W2015013753 abstract "1. Maize leaf inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC 3.6.1.1) exists as two major isozyme forms which are readily separable on polyacrylamide gel electrophoresis but are difficult to resolve by ion-exchange chromatography or isoelectric focusing. All 25 mutants examined had the same isozyme set; in 20 of these Isozyme 2 predominated and in the remaining five approximately equal amounts of Isozymes 1 and 2 were present. 2. Only Isozyme 2 is present in extracts of very young etiolated plants. Isozyme 1 could be obtained free of Isozyme 2 from light-grown seedlings treated with cycloheximide. 3. Isozymes 1 and 2 appeared to be similar in size and enzymatic properties, but thermal denaturation and immunological studies indicated that they have significant differences in structure. 4. These maize leaf pyrophosphatase isozymes and analogous enzymes from other plants have potent activity at pH 6.2 using Zn2+ as the activating metal ion, as well as their previously reported high activity at pH 9.0 with Mg2+. 5. Although leaf pyrophosphatase appears to be an integral part of the C4 pathway of CO2 fixation, metabolites of that pathway apparently have no regulatory effect upon the enzyme." @default.
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- W2015013753 date "1973-01-01" @default.
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- W2015013753 title "Maize leaf inorganic pyrophosphatase: Isozymes, specificity for substrates, inhibitors, and divalent metal ions, and pH optima" @default.
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- W2015013753 doi "https://doi.org/10.1016/0005-2744(73)90396-3" @default.
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