1992
DOI: 10.1016/s0176-1617(11)81076-x
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Characterization of the Peroxidase System in Winter Rye Seedlings:Compartmentation and Dependence on Leaf Development and Hydrogen Donors Used

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Cited by 6 publications
(2 citation statements)
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“…As described by Washko et al (1992), ascorbic acid oxidation in biological samples can be affected by numerous abiotic as well as enzymatic factors. Enzymes that directly or indirectly use ASC, such as ASC oxidase (Esaka et al, 1989) and peroxidases (Takahama and Oniki, 1992), are localized in the plant apoplast and are sometimes strongly bound to the cell wall fraction (Esaka et al, 1989;Ievinsh, 1992). Since it is possible that part of the cell wall fraction remains attached to the plasma membrane surface, it is also conceivable that some of these enzyme activities are still present in highly purified membrane preparations.…”
Section: Discussionmentioning
confidence: 99%
“…As described by Washko et al (1992), ascorbic acid oxidation in biological samples can be affected by numerous abiotic as well as enzymatic factors. Enzymes that directly or indirectly use ASC, such as ASC oxidase (Esaka et al, 1989) and peroxidases (Takahama and Oniki, 1992), are localized in the plant apoplast and are sometimes strongly bound to the cell wall fraction (Esaka et al, 1989;Ievinsh, 1992). Since it is possible that part of the cell wall fraction remains attached to the plasma membrane surface, it is also conceivable that some of these enzyme activities are still present in highly purified membrane preparations.…”
Section: Discussionmentioning
confidence: 99%
“…The reaction was initiated by adding 0.01 ml extract, and increase in A470 min -) was measured. Guaiacol was used as the substrate in this assay because it reacts with more isoforms of peroxidase than many other hydrogen donors (Ievinsh 1992), and because it remains in solution more readily than other substrates during the assay. Soluble protein in the homogenate was analyzed by the Bradford (1976) method.…”
Section: Total Soluble Plus Ionically Bound Peroxidase Activitymentioning
confidence: 99%