Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp

Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell fre...
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Autor*in:	Šeatović Svetlana [verfasserIn] Gligić Ljubinka [verfasserIn] Radulović Željka [verfasserIn] Jankov Ratko M. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2004

Schlagwörter:	superoxide dismutase thermothrix sp. isolation purification characterization

Übergeordnetes Werk:	In: Journal of the Serbian Chemical Society - Serbian Chemical Society, 2017, 69(2004), 1, Seite 9-16
Übergeordnetes Werk:	volume:69 ; year:2004 ; number:1 ; pages:9-16

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.2298/JSC0401009S

Katalog-ID:	DOAJ045900221

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spelling	10.2298/JSC0401009S doi (DE-627)DOAJ045900221 (DE-599)DOAJaaf98bb393a3441ab421264ccc2b26f0 DE-627 ger DE-627 rakwb eng QD1-999 Šeatović Svetlana verfasserin aut Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp 2004 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell free extract, was purified to homogenity by ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography and QAE Sephadex ion exchange chromatography. The specific activity of the purified enzyme was 9191 U/mg. The purified enzyme was analyzed and partially characterized. SOD was localized in polyacrylamide gel by activity staining, based on the reduction of nitroblue tetrazolium (NBT) by superoxide. The enzyme molecular weight determined by gel chromatography is 37 kD. According to SDS PAGE it is composed of two subunits of equal size, joined by noncovalent interactions. The isoelectric point, assessed by isoelectric focusing is 5.3. The optimum pH for enzyme activity was in the range of 8 to 10. The optimum temperature for SOD activity was 60 ºC. After one hour of incubation at 40, 50 and 60 ºC the SOD activity increases, but at 80 ºC, the SOD is denaturated. After 24 hours of incubation at 25 ºC SO Dactivity only slightly decreases. superoxide dismutase thermothrix sp. isolation purification characterization Chemistry Gligić Ljubinka verfasserin aut Radulović Željka verfasserin aut Jankov Ratko M. verfasserin aut In Journal of the Serbian Chemical Society Serbian Chemical Society, 2017 69(2004), 1, Seite 9-16 (DE-627)324742363 (DE-600)2030173-X 18207421 nnns volume:69 year:2004 number:1 pages:9-16 https://doi.org/10.2298/JSC0401009S kostenfrei https://doaj.org/article/aaf98bb393a3441ab421264ccc2b26f0 kostenfrei http://www.doiserbia.nb.rs/img/doi/0352-5139/2004/0352-51390401009S.pdf kostenfrei https://doaj.org/toc/0352-5139 Journal toc kostenfrei https://doaj.org/toc/1820-7421 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 69 2004 1 9-16
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callnumber-first	Q - Science
author	Šeatović Svetlana
spellingShingle	Šeatović Svetlana misc QD1-999 misc superoxide dismutase misc thermothrix sp. misc isolation misc purification misc characterization misc Chemistry Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp
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topic_title	QD1-999 Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp superoxide dismutase thermothrix sp isolation purification characterization
topic	misc QD1-999 misc superoxide dismutase misc thermothrix sp. misc isolation misc purification misc characterization misc Chemistry
topic_unstemmed	misc QD1-999 misc superoxide dismutase misc thermothrix sp. misc isolation misc purification misc characterization misc Chemistry
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title	Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp
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title_full	Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp
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author_browse	Šeatović Svetlana Gligić Ljubinka Radulović Željka Jankov Ratko M.
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title_sort	purification and partial characterization of superoxide dismutase from the thermophilic bacteria thermothrix sp
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title_auth	Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp
abstract	Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell free extract, was purified to homogenity by ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography and QAE Sephadex ion exchange chromatography. The specific activity of the purified enzyme was 9191 U/mg. The purified enzyme was analyzed and partially characterized. SOD was localized in polyacrylamide gel by activity staining, based on the reduction of nitroblue tetrazolium (NBT) by superoxide. The enzyme molecular weight determined by gel chromatography is 37 kD. According to SDS PAGE it is composed of two subunits of equal size, joined by noncovalent interactions. The isoelectric point, assessed by isoelectric focusing is 5.3. The optimum pH for enzyme activity was in the range of 8 to 10. The optimum temperature for SOD activity was 60 ºC. After one hour of incubation at 40, 50 and 60 ºC the SOD activity increases, but at 80 ºC, the SOD is denaturated. After 24 hours of incubation at 25 ºC SO Dactivity only slightly decreases.
abstractGer	Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell free extract, was purified to homogenity by ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography and QAE Sephadex ion exchange chromatography. The specific activity of the purified enzyme was 9191 U/mg. The purified enzyme was analyzed and partially characterized. SOD was localized in polyacrylamide gel by activity staining, based on the reduction of nitroblue tetrazolium (NBT) by superoxide. The enzyme molecular weight determined by gel chromatography is 37 kD. According to SDS PAGE it is composed of two subunits of equal size, joined by noncovalent interactions. The isoelectric point, assessed by isoelectric focusing is 5.3. The optimum pH for enzyme activity was in the range of 8 to 10. The optimum temperature for SOD activity was 60 ºC. After one hour of incubation at 40, 50 and 60 ºC the SOD activity increases, but at 80 ºC, the SOD is denaturated. After 24 hours of incubation at 25 ºC SO Dactivity only slightly decreases.
abstract_unstemmed	Superoxide dismutase (SOD; EC 1.15.1.1), a high molecular weight component of the antioxidant defense system, provided promising results in the treatment of oxidative damage. Thermothrix sp., isolated from thermal spa water in Serbia, showed high superoxide dismutase activity. The SOD, from cell free extract, was purified to homogenity by ammonium sulfate precipitation, Sephadex G 75 gel filtration chromatography and QAE Sephadex ion exchange chromatography. The specific activity of the purified enzyme was 9191 U/mg. The purified enzyme was analyzed and partially characterized. SOD was localized in polyacrylamide gel by activity staining, based on the reduction of nitroblue tetrazolium (NBT) by superoxide. The enzyme molecular weight determined by gel chromatography is 37 kD. According to SDS PAGE it is composed of two subunits of equal size, joined by noncovalent interactions. The isoelectric point, assessed by isoelectric focusing is 5.3. The optimum pH for enzyme activity was in the range of 8 to 10. The optimum temperature for SOD activity was 60 ºC. After one hour of incubation at 40, 50 and 60 ºC the SOD activity increases, but at 80 ºC, the SOD is denaturated. After 24 hours of incubation at 25 ºC SO Dactivity only slightly decreases.
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title_short	Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp
url	https://doi.org/10.2298/JSC0401009S https://doaj.org/article/aaf98bb393a3441ab421264ccc2b26f0 http://www.doiserbia.nb.rs/img/doi/0352-5139/2004/0352-51390401009S.pdf https://doaj.org/toc/0352-5139 https://doaj.org/toc/1820-7421
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up_date	2024-07-03T17:41:59.209Z
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Purification and partial characterization of superoxide dismutase from the thermophilic bacteria Thermothrix sp

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