Please use this identifier to cite or link to this item: https://biore.bio.bg.ac.rs/handle/123456789/98
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dc.contributor.authorHadži-Tašković Šukalović, Vesnaen_US
dc.contributor.authorVuletić, Mirjanaen_US
dc.contributor.authorMarković, Ksenijaen_US
dc.contributor.authorCvetić Antić, Tijanaen_US
dc.contributor.authorVučinić, Željkoen_US
dc.date.accessioned2019-06-19T20:24:36Z-
dc.date.available2019-06-19T20:24:36Z-
dc.date.issued2014-01-01-
dc.identifier.issn0033-183X-
dc.identifier.urihttps://biore.bio.bg.ac.rs/handle/123456789/98-
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 H<inf>2</inf>O<inf>2</inf>, 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_US
dc.language.isoenen_US
dc.relationOI 173040en_US
dc.relation.ispartofProtoplasmaen_US
dc.subjectAlkaline extractionen_US
dc.subjectCell wall peroxidaseen_US
dc.subjectEnzymatic digestionen_US
dc.subjectEnzyme covalent bindingen_US
dc.subjectMaize rooten_US
dc.subjectZea maysen_US
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_US
dc.typeArticleen_US
dc.identifier.doi10.1007/s00709-014-0684-2-
dc.identifier.pmid25081230-
dc.identifier.scopus2-s2.0-84939885609-
dc.identifier.urlhttps://api.elsevier.com/content/abstract/scopus_id/84939885609-
item.languageiso639-1en-
item.cerifentitytypePublications-
item.openairetypeArticle-
item.fulltextWith Fulltext-
item.grantfulltextrestricted-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.author.deptChair of Plant Physiology-
crisitem.author.orcid0000-0003-1676-7508-
Appears in Collections:Journal Article
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