caa a22 4500 477100651 CHVBK 20180405111540.0 cr unu---uuuuu 170330e19960101xx s 000 0 eng 10.1007/BF00197587 doi (NATIONALLICENCE)springer-10.1007/BF00197587 Cytosolic ascorbate peroxidase from Arabidopsis thaliana L. is encoded by a small multigene family [Elektronische Daten] [Maria Santos, Helene Gousseau, Clare Lister, Christine Foyer, Gary Creissen, Philip Mullineaux] A second cytosolic ascorbate peroxidase (cAPX; EC 1.11.1.11) gene from Arabidopsis thaliana has been characterised. This second gene (designated APX1b) maps to linkage group 3 and potentially encodes a cAPX as closely related to that from other dicotyledonous species as to the other member of this gene family (Kubo et al, 1993, FEBS Lett 315: 313-317; here designated APX1a), which maps to linkage group 1. In contrast, the lack of sequence similarity in non-coding regions of the genes implies that they are differentially regulated. Under non-stressed conditions only APX1a is expressed. APX1b was identified during low-stringency probing using a cDNA coding for pea cAPX which, in turn, was recovered from a cDNA library by immunoscreening with an antiserum raised against tea plastidial APX (pAPX). No pAPX cDNAs were recovered, despite the antiserum displaying specificity for pAPX in Western blots. Springer-Verlag, 1996 Arabidopsis nationallicence Ascorbate peroxidase (cytosolic, plastidial) nationallicence Multigene family nationallicence Oxidative stress nationallicence Pisum nationallicence ATG : methionine translation initiation codon nationallicence bp : base pair nationallicence cAPX : cytosolic ascorbate peroxidase nationallicence pAPX : plastidial ascorbate peroxidase nationallicence RFLP : restriction fragment length polymorphism nationallicence Santos Maria John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut Gousseau Helene Laboratoire de Metabolisme, INRA, Centre de Recherches de Versailles, F-78026, Versailles, France aut Lister Clare John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut Foyer Christine Laboratoire de Metabolisme, INRA, Centre de Recherches de Versailles, F-78026, Versailles, France aut Creissen Gary John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut Mullineaux Philip John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut Planta Springer-Verlag 198/1(1996-01-01), 64-69 0032-0935 198:1<64 1996 198 425 https://doi.org/10.1007/BF00197587 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00197587 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Santos Maria John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut NATIONALLICENCE 700 1- Gousseau Helene Laboratoire de Metabolisme, INRA, Centre de Recherches de Versailles, F-78026, Versailles, France aut NATIONALLICENCE 700 1- Lister Clare John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut NATIONALLICENCE 700 1- Foyer Christine Laboratoire de Metabolisme, INRA, Centre de Recherches de Versailles, F-78026, Versailles, France aut NATIONALLICENCE 700 1- Creissen Gary John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut NATIONALLICENCE 700 1- Mullineaux Philip John Innes Centre, Norwich Research Park, NR4 7UH, Colney, Norwich, UK aut NATIONALLICENCE 773 0- Planta Springer-Verlag 198/1(1996-01-01), 64-69 0032-0935 198:1<64 1996 198 425 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer