Regulation and function of ascorbate peroxidase isoenzymes

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Regulation and function of ascorbate peroxidase isoenzymes.

Even under optimal conditions, many metabolic processes, including the chloroplastic, mitochondrial, and plasma membrane-linked electron transport systems of higher plants, produce active oxygen species (AOS). Furthermore, the imposition of biotic and abiotic stress conditions can give rise to excess concentrations of AOS, resulting in oxidative damage at the cellular level. Therefore, antioxid...

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Alternatively spliced mRNA variants of chloroplast ascorbate peroxidase isoenzymes in spinach leaves.

We have previously shown that stromal and thylakoid-bound ascorbate peroxidase (APX) isoenzymes of spinach chloroplasts arise from a common pre-mRNA by alternative splicing in the C-terminus of the isoenzymes [Ishikawa, Yoshimura, Tamoi, Takeda and Shigeoka (1997) Biochem. J. 328, 795-800]. To explore the production of mature, functional mRNA encoding chloroplast APX isoenzymes, reverse transcr...

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Alternative mRNA splicing of 3'-terminal exons generates ascorbate peroxidase isoenzymes in spinach (Spinacia oleracea) chloroplasts.

We have isolated two cDNA clones encoding spinach (Spinacia oleracea) stromal and thylakoid-bound ascorbate peroxidase isoenzymes [Ishikawa, Sakai, Yoshimura, Takeda and Shigeoka (1996) FEBS Lett. 384, 289-293]. The gene (ApxII) encoding both chloroplastic ascorbate peroxidase isoenzymes was isolated and the organization of the gene was determined. Alignment between the cDNAs and the gene for c...

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Expression of spinach ascorbate peroxidase isoenzymes in response to oxidative stresses.

We studied the response of each ascorbate peroxidase (APX) isoenzyme in spinach leaves under stress conditions imposed by high light intensity, drought, salinity, and applications of methyl viologen and abscisic acid. The steady-state transcript level of cytosolic APX remarkably increased in response to high-light stress and methyl viologen treatment, but not in response to the other stress tre...

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Peroxidase Isoenzymes from Horseradish Roots

The reactivity of histidine in horseradish peroxidase isoenzymes Al and C was determined by titrating with diazonium-lH-tetrazole. No exposed histidine residue was detected in the native isoenzymes. Upon removal of the heme prosthetic group, however, all three histidine residues became titratable. Studies with p-chloromercuribenzoate and 14C-iodoacetamide indicated that the 6 half-cystine resid...

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ژورنال

عنوان ژورنال: Journal of Experimental Botany

سال: 2002

ISSN: 1460-2431

DOI: 10.1093/jexbot/53.372.1305