Vučinić, Željko

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  • Vučinić, Željko (5)
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Author's Bibliography

Modification of antioxidant systems in cell walls of maize roots by different nitrogen sources

Hadži-Tašković-Šukalović, Vesna; Vučinić, Željko; Vuletić, Mirjana; Marković, Ksenija; Kravić, Natalija

(Spanish Natl Inst Agricultural & Food Research & Technolo, Madrid, 2016)

TY  - JOUR
AU  - Hadži-Tašković-Šukalović, Vesna
AU  - Vučinić, Željko
AU  - Vuletić, Mirjana
AU  - Marković, Ksenija
AU  - Kravić, Natalija
PY  - 2016
UR  - http://rik.mrizp.rs/handle/123456789/618
AB  - Antioxidant systems of maize root cell walls grown on different nitrogen sources were evaluated. Plants were grown on a medium containing only NO3- or the mixture of NO3-+NH4+, in a 2:1 ratio. Eleven-day old plants, two days after the initiation of lateral roots, were used for the experiments. Cell walls were isolated from lateral roots and primary root segments, 2-7 cm from tip to base, representing zones of intense or decreased growth rates, respectively. Protein content and the activity of enzymes peroxidase, malate dehydrogenase and ascorbate oxidase ionically or covalently bound to the walls, as well as cell wall phenolic content and antioxidant capacity, were determined. Cell walls of plants grown on mixed N possess more developed enzymatic antioxidant systems and lower non-enzymatic antioxidant defenses than cell walls grown on NO3-. Irrespective of N treatment, the activities of all studied enzymes and protein content were higher in cell walls of lateral compared to primary roots. Phenolic content of cell walls isolated from lateral roots was higher in NO3--grown than in mixed N grown plants. No significant differences could be observed in the isozyme patterns of cell wall peroxidases isolated from plants grown on different nutrient solution. Our results indicate that different N treatments modify the antioxidant systems of root cell walls. Treatment with NO3- resulted in an increase of constitutive phenolic content, while the combination of NO3-+NH4+ elevated the redox enzyme activities in root cell walls.
PB  - Spanish Natl Inst Agricultural & Food Research & Technolo, Madrid
T2  - Spanish Journal of Agricultural Research
T1  - Modification of antioxidant systems in cell walls of maize roots by different nitrogen sources
VL  - 14
IS  - 4
DO  - 10.5424/sjar/2016144-8305
ER  - 
@article{
author = "Hadži-Tašković-Šukalović, Vesna and Vučinić, Željko and Vuletić, Mirjana and Marković, Ksenija and Kravić, Natalija",
year = "2016",
url = "http://rik.mrizp.rs/handle/123456789/618",
abstract = "Antioxidant systems of maize root cell walls grown on different nitrogen sources were evaluated. Plants were grown on a medium containing only NO3- or the mixture of NO3-+NH4+, in a 2:1 ratio. Eleven-day old plants, two days after the initiation of lateral roots, were used for the experiments. Cell walls were isolated from lateral roots and primary root segments, 2-7 cm from tip to base, representing zones of intense or decreased growth rates, respectively. Protein content and the activity of enzymes peroxidase, malate dehydrogenase and ascorbate oxidase ionically or covalently bound to the walls, as well as cell wall phenolic content and antioxidant capacity, were determined. Cell walls of plants grown on mixed N possess more developed enzymatic antioxidant systems and lower non-enzymatic antioxidant defenses than cell walls grown on NO3-. Irrespective of N treatment, the activities of all studied enzymes and protein content were higher in cell walls of lateral compared to primary roots. Phenolic content of cell walls isolated from lateral roots was higher in NO3--grown than in mixed N grown plants. No significant differences could be observed in the isozyme patterns of cell wall peroxidases isolated from plants grown on different nutrient solution. Our results indicate that different N treatments modify the antioxidant systems of root cell walls. Treatment with NO3- resulted in an increase of constitutive phenolic content, while the combination of NO3-+NH4+ elevated the redox enzyme activities in root cell walls.",
publisher = "Spanish Natl Inst Agricultural & Food Research & Technolo, Madrid",
journal = "Spanish Journal of Agricultural Research",
title = "Modification of antioxidant systems in cell walls of maize roots by different nitrogen sources",
volume = "14",
number = "4",
doi = "10.5424/sjar/2016144-8305"
}
Hadži-Tašković-Šukalović, V., Vučinić, Ž., Vuletić, M., Marković, K.,& Kravić, N. (2016). Modification of antioxidant systems in cell walls of maize roots by different nitrogen sources.
Spanish Journal of Agricultural Research
Spanish Natl Inst Agricultural & Food Research & Technolo, Madrid., 14(4).
https://doi.org/10.5424/sjar/2016144-8305
Hadži-Tašković-Šukalović V, Vučinić Ž, Vuletić M, Marković K, Kravić N. Modification of antioxidant systems in cell walls of maize roots by different nitrogen sources. Spanish Journal of Agricultural Research. 2016;14(4)
Hadži-Tašković-Šukalović Vesna, Vučinić Željko, Vuletić Mirjana, Marković Ksenija, Kravić Natalija, "Modification of antioxidant systems in cell walls of maize roots by different nitrogen sources" Spanish Journal of Agricultural Research, 14, no. 4 (2016),
https://doi.org/10.5424/sjar/2016144-8305 .
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Comparative biochemical characterization of peroxidases (class III) tightly bound to the maize root cell walls and modulation of the enzyme properties as a result of covalent binding

Hadži-Tašković-Šukalović, Vesna; Vučinić, Željko; Vuletić, Mirjana; Marković, Ksenija; Cvetic-Antić, Tijana

(Springer Wien, Wien, 2015)

TY  - JOUR
AU  - Hadži-Tašković-Šukalović, Vesna
AU  - Vučinić, Željko
AU  - Vuletić, Mirjana
AU  - Marković, Ksenija
AU  - Cvetic-Antić, Tijana
PY  - 2015
UR  - http://rik.mrizp.rs/handle/123456789/591
AB  - Comparative biochemical characterization of class III peroxidase activity tightly bound to the cell walls of maize roots was performed. Ionically bound proteins were solubilized from isolated walls by salt washing, and the remaining covalently bound peroxidases were released, either by enzymatic digestion or by a novel alkaline extraction procedure that released covalently bound alkali-resistant peroxidase enzyme. Solubilized fractions, as well as the salt-washed cell wall fragments containing covalently bound proteins, were analyzed for peroxidase activity. Peroxidative and oxidative activities indicated that peroxidase enzymes were predominately associated with walls by ionic interactions, and this fraction differs from the covalently bound one according to molecular weight, isozyme patterns, and biochemical parameters. The effect of covalent binding was evaluated by comparison of the catalytic properties of the enzyme bound to the salt-washed cell wall fragments with the corresponding solubilized and released enzyme. Higher thermal stability, improved resistance to KCN, increased susceptibility to H2O2, stimulated capacity of wall-bound enzyme to oxidize indole-3-acetic acid (IAA) as well as the difference in kinetic parameters between free and bound enzymes point to conformational changes due to covalent binding. Differences in biochemical properties of ionically and covalently bound peroxidases, as well as the modulation of the enzyme properties as a result of covalent binding to the walls, indicate that these two fractions of apoplastic peroxidases play different roles.
PB  - Springer Wien, Wien
T2  - Protoplasma
T1  - Comparative biochemical characterization of peroxidases (class III) tightly bound to the maize root cell walls and modulation of the enzyme properties as a result of covalent binding
VL  - 252
IS  - 1
SP  - 335
EP  - 343
DO  - 10.1007/s00709-014-0684-2
ER  - 
@article{
author = "Hadži-Tašković-Šukalović, Vesna and Vučinić, Željko and Vuletić, Mirjana and Marković, Ksenija and Cvetic-Antić, Tijana",
year = "2015",
url = "http://rik.mrizp.rs/handle/123456789/591",
abstract = "Comparative biochemical characterization of class III peroxidase activity tightly bound to the cell walls of maize roots was performed. Ionically bound proteins were solubilized from isolated walls by salt washing, and the remaining covalently bound peroxidases were released, either by enzymatic digestion or by a novel alkaline extraction procedure that released covalently bound alkali-resistant peroxidase enzyme. Solubilized fractions, as well as the salt-washed cell wall fragments containing covalently bound proteins, were analyzed for peroxidase activity. Peroxidative and oxidative activities indicated that peroxidase enzymes were predominately associated with walls by ionic interactions, and this fraction differs from the covalently bound one according to molecular weight, isozyme patterns, and biochemical parameters. The effect of covalent binding was evaluated by comparison of the catalytic properties of the enzyme bound to the salt-washed cell wall fragments with the corresponding solubilized and released enzyme. Higher thermal stability, improved resistance to KCN, increased susceptibility to H2O2, stimulated capacity of wall-bound enzyme to oxidize indole-3-acetic acid (IAA) as well as the difference in kinetic parameters between free and bound enzymes point to conformational changes due to covalent binding. Differences in biochemical properties of ionically and covalently bound peroxidases, as well as the modulation of the enzyme properties as a result of covalent binding to the walls, indicate that these two fractions of apoplastic peroxidases play different roles.",
publisher = "Springer Wien, Wien",
journal = "Protoplasma",
title = "Comparative biochemical characterization of peroxidases (class III) tightly bound to the maize root cell walls and modulation of the enzyme properties as a result of covalent binding",
volume = "252",
number = "1",
pages = "335-343",
doi = "10.1007/s00709-014-0684-2"
}
Hadži-Tašković-Šukalović, V., Vučinić, Ž., Vuletić, M., Marković, K.,& Cvetic-Antić, T. (2015). Comparative biochemical characterization of peroxidases (class III) tightly bound to the maize root cell walls and modulation of the enzyme properties as a result of covalent binding.
Protoplasma
Springer Wien, Wien., 252(1), 335-343.
https://doi.org/10.1007/s00709-014-0684-2
Hadži-Tašković-Šukalović V, Vučinić Ž, Vuletić M, Marković K, Cvetic-Antić T. Comparative biochemical characterization of peroxidases (class III) tightly bound to the maize root cell walls and modulation of the enzyme properties as a result of covalent binding. Protoplasma. 2015;252(1):335-343
Hadži-Tašković-Šukalović Vesna, Vučinić Željko, Vuletić Mirjana, Marković Ksenija, Cvetic-Antić Tijana, "Comparative biochemical characterization of peroxidases (class III) tightly bound to the maize root cell walls and modulation of the enzyme properties as a result of covalent binding" Protoplasma, 252, no. 1 (2015):335-343,
https://doi.org/10.1007/s00709-014-0684-2 .
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Differential response of antioxidative systems of maize (Zea mays L.) roots cell walls to osmotic and heavy metal stress

Vuletić, Mirjana; Marković, Ksenija; Kravić, Natalija; Hadži-Tašković-Šukalović, Vesna; Vučinić, Željko; Maksimović, Vuk

(Wiley-Blackwell, Hoboken, 2014)

TY  - JOUR
AU  - Vuletić, Mirjana
AU  - Marković, Ksenija
AU  - Kravić, Natalija
AU  - Hadži-Tašković-Šukalović, Vesna
AU  - Vučinić, Željko
AU  - Maksimović, Vuk
PY  - 2014
UR  - http://rik.mrizp.rs/handle/123456789/551
AB  - An analysis of peroxidase and ascorbate oxidase activity, phenolic content and antioxidant capacity of isolated maize root cell walls was performed in controls and plants stressed with polyethylene glycol (PEG) or heavy metals, zinc or copper. Peroxidase activity (oxidative and peroxidative) was more pronounced in the ionic than in the covalent cell wall fraction. PEG induced an increase and Zn2+ a decrease of both ionically bound peroxidase activities. In the covalent fraction, Cu2+ decreased oxidative and increased peroxidative activity of peroxidase. Isoelectric focusing of ionically bound proteins and activity staining for peroxidase demonstrated increased intensities and appearance of new acidic isoforms, especially in Zn2+ and PEG treatments. Most pronounced basic isoforms (pI similar to 7.5) in controls, decreased in intensity or completely disappeared in stressed plants. Ascorbate oxidase activity was significantly increased by PEG and decreased by Zn2+ treatments, and highly correlated with peroxidase activity. Antioxidant capacity and total phenolics content increased in heavy metal-treated and decreased in PEG-treated plants. Analysis of individual phenolic components revealed p-coumaric and ferulic acids, as the most abundant, as well as ferulic acid dimers, trimers and tetramers in the cell walls; their quantity increased under stress conditions. Results presented demonstrate the existence of diverse mechanisms of plant response to different stresses.
PB  - Wiley-Blackwell, Hoboken
T2  - Plant Biology
T1  - Differential response of antioxidative systems of maize (Zea mays L.) roots cell walls to osmotic and heavy metal stress
VL  - 16
IS  - 1
SP  - 88
EP  - 96
DO  - 10.1111/plb.12017
ER  - 
@article{
author = "Vuletić, Mirjana and Marković, Ksenija and Kravić, Natalija and Hadži-Tašković-Šukalović, Vesna and Vučinić, Željko and Maksimović, Vuk",
year = "2014",
url = "http://rik.mrizp.rs/handle/123456789/551",
abstract = "An analysis of peroxidase and ascorbate oxidase activity, phenolic content and antioxidant capacity of isolated maize root cell walls was performed in controls and plants stressed with polyethylene glycol (PEG) or heavy metals, zinc or copper. Peroxidase activity (oxidative and peroxidative) was more pronounced in the ionic than in the covalent cell wall fraction. PEG induced an increase and Zn2+ a decrease of both ionically bound peroxidase activities. In the covalent fraction, Cu2+ decreased oxidative and increased peroxidative activity of peroxidase. Isoelectric focusing of ionically bound proteins and activity staining for peroxidase demonstrated increased intensities and appearance of new acidic isoforms, especially in Zn2+ and PEG treatments. Most pronounced basic isoforms (pI similar to 7.5) in controls, decreased in intensity or completely disappeared in stressed plants. Ascorbate oxidase activity was significantly increased by PEG and decreased by Zn2+ treatments, and highly correlated with peroxidase activity. Antioxidant capacity and total phenolics content increased in heavy metal-treated and decreased in PEG-treated plants. Analysis of individual phenolic components revealed p-coumaric and ferulic acids, as the most abundant, as well as ferulic acid dimers, trimers and tetramers in the cell walls; their quantity increased under stress conditions. Results presented demonstrate the existence of diverse mechanisms of plant response to different stresses.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Plant Biology",
title = "Differential response of antioxidative systems of maize (Zea mays L.) roots cell walls to osmotic and heavy metal stress",
volume = "16",
number = "1",
pages = "88-96",
doi = "10.1111/plb.12017"
}
Vuletić, M., Marković, K., Kravić, N., Hadži-Tašković-Šukalović, V., Vučinić, Ž.,& Maksimović, V. (2014). Differential response of antioxidative systems of maize (Zea mays L.) roots cell walls to osmotic and heavy metal stress.
Plant Biology
Wiley-Blackwell, Hoboken., 16(1), 88-96.
https://doi.org/10.1111/plb.12017
Vuletić M, Marković K, Kravić N, Hadži-Tašković-Šukalović V, Vučinić Ž, Maksimović V. Differential response of antioxidative systems of maize (Zea mays L.) roots cell walls to osmotic and heavy metal stress. Plant Biology. 2014;16(1):88-96
Vuletić Mirjana, Marković Ksenija, Kravić Natalija, Hadži-Tašković-Šukalović Vesna, Vučinić Željko, Maksimović Vuk, "Differential response of antioxidative systems of maize (Zea mays L.) roots cell walls to osmotic and heavy metal stress" Plant Biology, 16, no. 1 (2014):88-96,
https://doi.org/10.1111/plb.12017 .
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Cell wall-associated malate dehydrogenase activity from maize roots

Hadži-Tašković-Šukalović, Vesna; Vučinić, Željko; Vuletić, Mirjana; Marković, Ksenija

(Elsevier Ireland Ltd, Clare, 2011)

TY  - JOUR
AU  - Hadži-Tašković-Šukalović, Vesna
AU  - Vučinić, Željko
AU  - Vuletić, Mirjana
AU  - Marković, Ksenija
PY  - 2011
UR  - http://rik.mrizp.rs/handle/123456789/373
AB  - Isolated cell walls from maize (Zea mays L) roots exhibited ionically and covalently bound NAD-specific malate dehydrogenase activity. The enzyme catalyses a rapid reduction of oxaloacetate and much slower oxidation of malate. The kinetic and regulatory properties of the cell wall enzyme solubilized with 1 M NaCl were different from those published for soluble, mitochondrial or plasma membrane malate dehydrogenase with respect to their ATP, Pi, and pH dependence. Isoelectric focusing of ionically-bound proteins and specific staining for malate dehydrogenase revealed characteristic isoforms present in cell wall isolate, different from those present in plasma membranes and crude homogenate. Much greater activity of cell wall-associated malate dehydrogenase was detected in the intensively growing lateral roots compared to primary root with decreased growth rates. Presence of Zn2+ and Cu2+ in the assay medium inhibited the activity of the wall-associated malate dehydrogenase. Exposure of maize plants to excess concentrations of Zn2+ and Cu2+ in the hydroponic solution inhibited lateral root growth, decreased malate dehydrogenase activity and changed isoform profiles. The results presented show that cell wall malate dehydrogenase is truly a wall-bound enzyme, and not an artefact of cytoplasmic contamination, involved in the developmental processes, and detoxification of heavy metals.
PB  - Elsevier Ireland Ltd, Clare
T2  - Plant Science
T1  - Cell wall-associated malate dehydrogenase activity from maize roots
VL  - 181
IS  - 4
SP  - 465
EP  - 470
DO  - 10.1016/j.plantsci.2011.07.007
ER  - 
@article{
author = "Hadži-Tašković-Šukalović, Vesna and Vučinić, Željko and Vuletić, Mirjana and Marković, Ksenija",
year = "2011",
url = "http://rik.mrizp.rs/handle/123456789/373",
abstract = "Isolated cell walls from maize (Zea mays L) roots exhibited ionically and covalently bound NAD-specific malate dehydrogenase activity. The enzyme catalyses a rapid reduction of oxaloacetate and much slower oxidation of malate. The kinetic and regulatory properties of the cell wall enzyme solubilized with 1 M NaCl were different from those published for soluble, mitochondrial or plasma membrane malate dehydrogenase with respect to their ATP, Pi, and pH dependence. Isoelectric focusing of ionically-bound proteins and specific staining for malate dehydrogenase revealed characteristic isoforms present in cell wall isolate, different from those present in plasma membranes and crude homogenate. Much greater activity of cell wall-associated malate dehydrogenase was detected in the intensively growing lateral roots compared to primary root with decreased growth rates. Presence of Zn2+ and Cu2+ in the assay medium inhibited the activity of the wall-associated malate dehydrogenase. Exposure of maize plants to excess concentrations of Zn2+ and Cu2+ in the hydroponic solution inhibited lateral root growth, decreased malate dehydrogenase activity and changed isoform profiles. The results presented show that cell wall malate dehydrogenase is truly a wall-bound enzyme, and not an artefact of cytoplasmic contamination, involved in the developmental processes, and detoxification of heavy metals.",
publisher = "Elsevier Ireland Ltd, Clare",
journal = "Plant Science",
title = "Cell wall-associated malate dehydrogenase activity from maize roots",
volume = "181",
number = "4",
pages = "465-470",
doi = "10.1016/j.plantsci.2011.07.007"
}
Hadži-Tašković-Šukalović, V., Vučinić, Ž., Vuletić, M.,& Marković, K. (2011). Cell wall-associated malate dehydrogenase activity from maize roots.
Plant Science
Elsevier Ireland Ltd, Clare., 181(4), 465-470.
https://doi.org/10.1016/j.plantsci.2011.07.007
Hadži-Tašković-Šukalović V, Vučinić Ž, Vuletić M, Marković K. Cell wall-associated malate dehydrogenase activity from maize roots. Plant Science. 2011;181(4):465-470
Hadži-Tašković-Šukalović Vesna, Vučinić Željko, Vuletić Mirjana, Marković Ksenija, "Cell wall-associated malate dehydrogenase activity from maize roots" Plant Science, 181, no. 4 (2011):465-470,
https://doi.org/10.1016/j.plantsci.2011.07.007 .
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Plasma-membrane-bound malate dehydrogenase activity in maize roots

Hadži-Tašković-Šukalović, Vesna; Vuletić, Mirjana; Ignjatović-Micić, Dragana; Vučinić, Željko

(1999)

TY  - JOUR
AU  - Hadži-Tašković-Šukalović, Vesna
AU  - Vuletić, Mirjana
AU  - Ignjatović-Micić, Dragana
AU  - Vučinić, Željko
PY  - 1999
UR  - http://rik.mrizp.rs/handle/123456789/6
AB  - Plasma membranes were isolated and purified from 14-day-old maize roots (Zea mays L.) by two-phase partitioning at a 6.5% polymer concentration, and compared to isolated mitochondria, microsomes, and soluble fraction. Marker enzyme analysis demonstrated that the plasma membranes were devoid of cytoplasmic, mitochondrial, tonoplast, and endoplasmic-reticulum contaminations. Isolated plasma membranes exhibited malate dehydrogenase activity, catalyzing NADH-dependent reduction of oxaloacetate as well as NAD + -dependent malate oxidation. Malate dehydrogenase activity was resistant to osmotic shock, freeze-thaw treatment, and salt washing and stimulated by solubilization with Triton X-100, indicating that the enzyme is tightly bound to the plasma membrane. Malate dehydrogenase activity was highly specific to NAD + and NADH. The enzyme exhibited a high degree of latency in both right-side-out (80%) and inside-out (70%) vesicle preparations. Kinetic and regulatory properties with ATP and P(i), as well as pH dependence of plasma-membrane-bound malate dehydrogenase were different from mitochondrial and soluble malate dehydrogenases. Starch gel electrophoresis revealed a characteristic isozyme form present in the plasma membrane isolate, but not present in the soluble, mitochondrial, and microsomal fractions. The results presented show that purified plasma membranes isolated from maize roots contain a tightly associated malate dehydrogenase, having properties different from mitochondrial and soluble malate dehydrogenases.
T2  - Protoplasma
T1  - Plasma-membrane-bound malate dehydrogenase activity in maize roots
VL  - 207
IS  - 3-4
SP  - 203
EP  - 212
ER  - 
@article{
author = "Hadži-Tašković-Šukalović, Vesna and Vuletić, Mirjana and Ignjatović-Micić, Dragana and Vučinić, Željko",
year = "1999",
url = "http://rik.mrizp.rs/handle/123456789/6",
abstract = "Plasma membranes were isolated and purified from 14-day-old maize roots (Zea mays L.) by two-phase partitioning at a 6.5% polymer concentration, and compared to isolated mitochondria, microsomes, and soluble fraction. Marker enzyme analysis demonstrated that the plasma membranes were devoid of cytoplasmic, mitochondrial, tonoplast, and endoplasmic-reticulum contaminations. Isolated plasma membranes exhibited malate dehydrogenase activity, catalyzing NADH-dependent reduction of oxaloacetate as well as NAD + -dependent malate oxidation. Malate dehydrogenase activity was resistant to osmotic shock, freeze-thaw treatment, and salt washing and stimulated by solubilization with Triton X-100, indicating that the enzyme is tightly bound to the plasma membrane. Malate dehydrogenase activity was highly specific to NAD + and NADH. The enzyme exhibited a high degree of latency in both right-side-out (80%) and inside-out (70%) vesicle preparations. Kinetic and regulatory properties with ATP and P(i), as well as pH dependence of plasma-membrane-bound malate dehydrogenase were different from mitochondrial and soluble malate dehydrogenases. Starch gel electrophoresis revealed a characteristic isozyme form present in the plasma membrane isolate, but not present in the soluble, mitochondrial, and microsomal fractions. The results presented show that purified plasma membranes isolated from maize roots contain a tightly associated malate dehydrogenase, having properties different from mitochondrial and soluble malate dehydrogenases.",
journal = "Protoplasma",
title = "Plasma-membrane-bound malate dehydrogenase activity in maize roots",
volume = "207",
number = "3-4",
pages = "203-212"
}
Hadži-Tašković-Šukalović, V., Vuletić, M., Ignjatović-Micić, D.,& Vučinić, Ž. (1999). Plasma-membrane-bound malate dehydrogenase activity in maize roots.
Protoplasma, 207(3-4), 203-212.
Hadži-Tašković-Šukalović V, Vuletić M, Ignjatović-Micić D, Vučinić Ž. Plasma-membrane-bound malate dehydrogenase activity in maize roots. Protoplasma. 1999;207(3-4):203-212
Hadži-Tašković-Šukalović Vesna, Vuletić Mirjana, Ignjatović-Micić Dragana, Vučinić Željko, "Plasma-membrane-bound malate dehydrogenase activity in maize roots" Protoplasma, 207, no. 3-4 (1999):203-212
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