Cvetic-Antić, Tijana

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  • Cvetic-Antić, Tijana (1)
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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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