Distribution of the Mo-enzymes aldehyde oxidase, xanthine dehydrogenase and nitrate reductase in maize (Zea mays L.) nodal roots as affected by nitrogen and salinity

N. Katalin Barabás, Rustem T. Omarov, L. Erdei, S. Herman Lips

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

The distribution of the Mo-enzymes aldehyde oxidase (AO; EC 1.2.3.1) xanthine dehydrogenase (XDH; EC 1.2.1.37) and nitrate reductase (NAD(P)H NR; EC 1.6.6.1-2) was studied along the longitudinal and transversal axes of maize (Zea mays L. cv. Jubily) nodal roots as affected by nitrogen sources and salinity. Activities of the Mo-enzymes were considerably enhanced under mild saline conditions. The activities of AO and XDH increased following addition of ammonium to the nutrient solution. Immunoblot analysis with antibodies raised against maize AO protein revealed increased levels AO proteins in root tips of ammonium fed plants. Application of salinity to nitrate fed plants did not affect the enzyme protein level, although it enhanced the activity of the Mo-hydroxylases. The specific activities of the Mo-enzymes were the highest in root tips (0-1 cm segments) while on the transversal axis maximal activity was observed in the stele or vascular cylinder. Activity staining of AO after native PAGE of root extracts revealed four bands of AO proteins (AO1-4) capable of oxidizing a number of aliphatic and aromatic aldehydes. Increased AO activity in maize nodal roots grown with ammonium, and salinity were observed mainly at the AO3 and AO4 bands. Tips and stele contained primarily AO3 and AO4, and only traces of AO1 and AO2. SDS-PAGE of root extracts followed by Western blots revealed, besides the major 150 kD subunit of AO, two polypeptides with molecular masses of 72 and 85 kD located specifically in the cortex. Part of the polymorphism of AO in plant roots may be related to the allocation of distinct isoforms to different regions of the root, although the specific metabolic roles of the different bands have not been established. (C) 2000 Elsevier Science Ireland Ltd.

Original languageEnglish
Pages (from-to)49-58
Number of pages10
JournalPlant Science
Volume155
Issue number1
DOIs
Publication statusPublished - Jun 12 2000

Fingerprint

Aldehyde Oxidase
Xanthine Dehydrogenase
xanthine dehydrogenase
Nitrate Reductase
Salinity
nitrate reductase
aldehydes
Zea mays
Nitrogen
Ammonium Compounds
salinity
corn
Meristem
nitrogen
Enzymes
enzymes
Nitrate Reductase (NAD(P)H)
stele
Proteins
Native Polyacrylamide Gel Electrophoresis

Keywords

  • Aldehyde oxidase
  • Cortex
  • Maize
  • Nitrate reductase
  • Nodal roots
  • Root tips
  • Stele
  • Xanthine dehydrogenase

ASJC Scopus subject areas

  • Plant Science
  • Biochemistry
  • Biotechnology

Cite this

Distribution of the Mo-enzymes aldehyde oxidase, xanthine dehydrogenase and nitrate reductase in maize (Zea mays L.) nodal roots as affected by nitrogen and salinity. / Katalin Barabás, N.; Omarov, Rustem T.; Erdei, L.; Herman Lips, S.

In: Plant Science, Vol. 155, No. 1, 12.06.2000, p. 49-58.

Research output: Contribution to journalArticle

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abstract = "The distribution of the Mo-enzymes aldehyde oxidase (AO; EC 1.2.3.1) xanthine dehydrogenase (XDH; EC 1.2.1.37) and nitrate reductase (NAD(P)H NR; EC 1.6.6.1-2) was studied along the longitudinal and transversal axes of maize (Zea mays L. cv. Jubily) nodal roots as affected by nitrogen sources and salinity. Activities of the Mo-enzymes were considerably enhanced under mild saline conditions. The activities of AO and XDH increased following addition of ammonium to the nutrient solution. Immunoblot analysis with antibodies raised against maize AO protein revealed increased levels AO proteins in root tips of ammonium fed plants. Application of salinity to nitrate fed plants did not affect the enzyme protein level, although it enhanced the activity of the Mo-hydroxylases. The specific activities of the Mo-enzymes were the highest in root tips (0-1 cm segments) while on the transversal axis maximal activity was observed in the stele or vascular cylinder. Activity staining of AO after native PAGE of root extracts revealed four bands of AO proteins (AO1-4) capable of oxidizing a number of aliphatic and aromatic aldehydes. Increased AO activity in maize nodal roots grown with ammonium, and salinity were observed mainly at the AO3 and AO4 bands. Tips and stele contained primarily AO3 and AO4, and only traces of AO1 and AO2. SDS-PAGE of root extracts followed by Western blots revealed, besides the major 150 kD subunit of AO, two polypeptides with molecular masses of 72 and 85 kD located specifically in the cortex. Part of the polymorphism of AO in plant roots may be related to the allocation of distinct isoforms to different regions of the root, although the specific metabolic roles of the different bands have not been established. (C) 2000 Elsevier Science Ireland Ltd.",
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AU - Katalin Barabás, N.

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AU - Herman Lips, S.

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