Peroxisomal membrane manganese superoxide dismutase : characterization of the isozyme from watermelon (Citrullus lanatus Schrad.) cotyledons

In this work the manganese superoxide dismutase (Mn-SOD) bound to peroxisomal membranes of watermelon cotyledons (Citrullus lanatus Schrad.) was purified to homogeneity and some of its molecular properties were determined. The stepwise purification procedure consisted of ammonium sulphate fractionat...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 58(2007), 10 vom: 14., Seite 2417-27
1. Verfasser: Rodríguez-Serrano, María (VerfasserIn)
Weitere Verfasser: Romero-Puertas, María C, Pastori, Gabriela M, Corpas, Francisco J, Sandalio, Luisa M, del Río, Luis A, Palma, José M
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Comparative Study Journal Article Research Support, Non-U.S. Gov't Isoenzymes Mitochondrial Proteins Plant Proteins Superoxide Dismutase EC 1.15.1.1
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100 1 |a Rodríguez-Serrano, María  |e verfasserin  |4 aut 
245 1 0 |a Peroxisomal membrane manganese superoxide dismutase  |b characterization of the isozyme from watermelon (Citrullus lanatus Schrad.) cotyledons 
264 1 |c 2007 
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500 |a Date Completed 02.01.2008 
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500 |a published: Print-Electronic 
500 |a ErratumIn: J Exp Bot. 2007;58(12):3483 
500 |a Citation Status MEDLINE 
520 |a In this work the manganese superoxide dismutase (Mn-SOD) bound to peroxisomal membranes of watermelon cotyledons (Citrullus lanatus Schrad.) was purified to homogeneity and some of its molecular properties were determined. The stepwise purification procedure consisted of ammonium sulphate fractionation, batch anion-exchange chromatography, and anion-exchange and gel-filtration column chromatography using a fast protein liquid chromatography system. Peroxisomal membrane Mn-SOD (perMn-SOD; EC 1.15.1.1) was purified 5600-fold with a yield of 2.6 mug of enzyme g(-1) of cotyledons, and had a specific activity of 480 U mg(-1) of protein. The native molecular mass determined for perMn-SOD was 108 000 Da, and it was composed of four equal subunits of 27 kDa, which indicates that perMn-SOD is a homotetramer. Ultraviolet and visible absorption spectra of the enzyme showed a shoulder at 275 nm and two absorption maxima at 448 nm and 555 nm, respectively. By isoelectric focusing, a pI of 5.75 was determined for perMn-SOD. In immunoblot assays, purified perMn-SOD was recognized by a polyclonal antibody against Mn-SOD from pea leaves, and the peroxisomal enzyme rapidly dissociated in the presence of dithiothreitol and SDS. The potential binding of the Mn-SOD isozyme to the peroxisomal membrane was confirmed by immunoelectron microscopy analysis. The properties of perMn-SOD and the mitMn-SOD are compared and the possible function in peroxisomal membranes of the peripheral protein Mn-SOD is discussed 
650 4 |a Comparative Study 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Isoenzymes  |2 NLM 
650 7 |a Mitochondrial Proteins  |2 NLM 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Superoxide Dismutase  |2 NLM 
650 7 |a EC 1.15.1.1  |2 NLM 
700 1 |a Romero-Puertas, María C  |e verfasserin  |4 aut 
700 1 |a Pastori, Gabriela M  |e verfasserin  |4 aut 
700 1 |a Corpas, Francisco J  |e verfasserin  |4 aut 
700 1 |a Sandalio, Luisa M  |e verfasserin  |4 aut 
700 1 |a del Río, Luis A  |e verfasserin  |4 aut 
700 1 |a Palma, José M  |e verfasserin  |4 aut 
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