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- W2054293467 abstract "Chloroplast glyceraldehyde-3-phosphate dehydrogenase (GPD, EC 1.2.1.13) was purified from leaves of Chenopodium rubrum L. Aggregated (≥ 106) and disaggregated (165 × 103) molecular weight forms were obtained by gel filtration in the presence of NAD+ and NADP+, respectively. The disaggregated enzyme was separated into two isozymes by inverse ammonium sulphate gradient solubilization: “NADP-GPD I” was homotetrameric (subunit molecular weight 39 × 103); “NADP-GPD II” was heterotetrameric (subunit molecular weights 39 × 103 and 43 × 103). Isoelectric focusing of the isozymes, both aggregated and disaggregated, revealed two isoelectric forms in each case, at 4.3 and 7.7. Chloroplast GPD was “NADP-suppressed” in crude extracts due to partial oxidation, incubation with dithioerythritol restored full activity." @default.
- W2054293467 created "2016-06-24" @default.
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- W2054293467 date "1983-02-01" @default.
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- W2054293467 title "In vitro and in vivo regulation of chloroplast glyceraldehydes-3-phosphate dehydrogenase isozymes from Chenopodium rubrum. I. Purification and properties of isozymes" @default.
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- W2054293467 doi "https://doi.org/10.1111/j.1399-3054.1983.tb00904.x" @default.
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