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- W2017332227 abstract "Abstract Approximately 4–5-fold stimulation of acid phosphatase activity was witnessed in embryo-less half-seeds of wheat in response to gibberellic acid (GA 3 ) (48 h). This enzyme activity was secreted into the incubation medium. The increase in enzyme activity in GA 3 -treated wheat half-seeds was inhibited significantly by cordycepin, cycloheximide (CHI) and amino acid analogues. This indicated the requirement of fresh transcription and translation for the GA 3 -regulated acid phosphatase activity. Abscisic acid completely abolished the GA 3 -induced acid phosphatase activity. Conclusive proof for de novo synthesis of acid phosphatase in GA 3 -treated half-seeds was achieved by the in vivo labelling of enzyme with [ 35 S]sulphate. The label was recovered in the cysteine residues of the purified enzyme. Acid phosphatase was purified (109-fold) to electrophoretic homogeneity by Con A-agarose affinity chromatography. The molecular weight of the native enzyme is 185 000 as determined by molecular sieve chromatography on Sepharose CL-6B. The K m of the enzyme for p -nitrophenyl phosphate is 5 × 10 −4 M. The pH optimum of the purified enzyme was 5.0. The enzyme activity was completely inhibited by NaF (2 mM). Both β-mercapto-ethanol (10 mM) and dithiothreitol (10 mM) brought about a 2.5–3-fold activation of acid phosphatase, thereby indicating the requirement of free sulfhydryl groups for the catalytic efficiency of the enzyme." @default.
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- W2017332227 date "1989-01-01" @default.
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- W2017332227 title "Regulation of acid phosphatase by gibberellic acid in embryo-less half-seeds of wheat" @default.
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- W2017332227 doi "https://doi.org/10.1016/0168-9452(89)90182-9" @default.
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