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dc.creatorHadži-Tašković-Šukalović, Vesna
dc.creatorVučinić, Željko
dc.creatorVuletić, Mirjana
dc.creatorMarković, Ksenija
dc.creatorCvetic-Antić, Tijana
dc.date.accessioned2019-05-16T12:18:36Z
dc.date.available2019-05-16T12:18:36Z
dc.date.issued2015
dc.identifier.issn0033-183X
dc.identifier.urihttp://rik.mrizp.rs/handle/123456789/591
dc.description.abstractComparative 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.en
dc.publisherSpringer Wien, Wien
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/173040/RS//
dc.rightsrestrictedAccess
dc.sourceProtoplasma
dc.subjectAlkaline extractionen
dc.subjectCell wall peroxidaseen
dc.subjectEnzymatic digestionen
dc.subjectEnzyme covalent bindingen
dc.subjectMaize rooten
dc.subjectZea maysen
dc.titleComparative 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 bindingen
dc.typearticle
dc.rights.licenseARR
dc.citation.volume252
dc.citation.issue1
dc.citation.spage335
dc.citation.epage343
dc.citation.other252(1): 335-343
dc.citation.rankM21
dc.identifier.wos000347704700030
dc.identifier.doi10.1007/s00709-014-0684-2
dc.identifier.pmid25081230
dc.identifier.scopus2-s2.0-84939885609
dc.type.versionpublishedVersion


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Приказ основних података о документу