Journal Article

Characterisation of Acidic and Basic Apoplastic Peroxidases from Needles of Norway Spruce (<i>Picea abies</i>, L., Karsten) with Respect to Lignifying Substrates

Tilman Otter and Andrea Polle

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 38, issue 5, pages 595-602
Published in print January 1997 | ISSN: 0032-0781
Published online January 1997 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/oxfordjournals.pcp.a029209
Characterisation of Acidic and Basic Apoplastic Peroxidases from Needles of Norway Spruce (Picea abies, L., Karsten) with Respect to Lignifying Substrates

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Acidic and basic peroxidases, termed as POD-A and POD-B, were isolated from the apoplastic space of spruce (Picea abies, L.) needles and purified by acetone precipitation and anion exchange chromatography to apparent homogeneity. The molecular masses of POD-A and POD-B were 39.6 and 29.0 kDa, respectively. The pH optimum of both isozymes ranged from 4.5 to 6. The apparent Km values of POD-A and POD-B were 460 and 210 μM for coniferyl alcohol. Both isozymes acted also as NADH oxidases with apparent Km-values of 103 μM (POD-A) and 70 μM (POD-B). NAD+ but not NADH was found in the apoplastic space of lignifying needles. Based on the lignification rate, the contents and kinetic properties of PODs, NADH oxidation by POD is not the major source of H2O2 required for lignin polymerisation.

Keywords: Apoplast; Cell wall; Lignification; NADH oxidase; Peroxidase (EC 1.11.1.7); Picea abies

Journal Article.  0 words. 

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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