Protein carbonylation detection methods: A comparison
The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11])...
Ausführliche Beschreibung
Autor*in: |
Esra'a Alomari [verfasserIn] Stefano Bruno [verfasserIn] Luca Ronda [verfasserIn] Gianluca Paredi [verfasserIn] Stefano Bettati [verfasserIn] Andrea Mozzarelli [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2018 |
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Übergeordnetes Werk: |
In: Data in Brief - Elsevier, 2015, 19(2018), Seite 2215-2220 |
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Übergeordnetes Werk: |
volume:19 ; year:2018 ; pages:2215-2220 |
Links: |
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DOI / URN: |
10.1016/j.dib.2018.06.088 |
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Katalog-ID: |
DOAJ075382814 |
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520 | |a The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. | ||
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allfields |
10.1016/j.dib.2018.06.088 doi (DE-627)DOAJ075382814 (DE-599)DOAJa0876f37da15420095422e55b34e61e7 DE-627 ger DE-627 rakwb eng R858-859.7 Q1-390 Esra'a Alomari verfasserin aut Protein carbonylation detection methods: A comparison 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. Computer applications to medicine. Medical informatics Science (General) Stefano Bruno verfasserin aut Luca Ronda verfasserin aut Gianluca Paredi verfasserin aut Stefano Bettati verfasserin aut Andrea Mozzarelli verfasserin aut In Data in Brief Elsevier, 2015 19(2018), Seite 2215-2220 (DE-627)797838937 (DE-600)2786545-9 23523409 nnns volume:19 year:2018 pages:2215-2220 https://doi.org/10.1016/j.dib.2018.06.088 kostenfrei https://doaj.org/article/a0876f37da15420095422e55b34e61e7 kostenfrei http://www.sciencedirect.com/science/article/pii/S235234091830739X kostenfrei https://doaj.org/toc/2352-3409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 19 2018 2215-2220 |
spelling |
10.1016/j.dib.2018.06.088 doi (DE-627)DOAJ075382814 (DE-599)DOAJa0876f37da15420095422e55b34e61e7 DE-627 ger DE-627 rakwb eng R858-859.7 Q1-390 Esra'a Alomari verfasserin aut Protein carbonylation detection methods: A comparison 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. Computer applications to medicine. Medical informatics Science (General) Stefano Bruno verfasserin aut Luca Ronda verfasserin aut Gianluca Paredi verfasserin aut Stefano Bettati verfasserin aut Andrea Mozzarelli verfasserin aut In Data in Brief Elsevier, 2015 19(2018), Seite 2215-2220 (DE-627)797838937 (DE-600)2786545-9 23523409 nnns volume:19 year:2018 pages:2215-2220 https://doi.org/10.1016/j.dib.2018.06.088 kostenfrei https://doaj.org/article/a0876f37da15420095422e55b34e61e7 kostenfrei http://www.sciencedirect.com/science/article/pii/S235234091830739X kostenfrei https://doaj.org/toc/2352-3409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 19 2018 2215-2220 |
allfields_unstemmed |
10.1016/j.dib.2018.06.088 doi (DE-627)DOAJ075382814 (DE-599)DOAJa0876f37da15420095422e55b34e61e7 DE-627 ger DE-627 rakwb eng R858-859.7 Q1-390 Esra'a Alomari verfasserin aut Protein carbonylation detection methods: A comparison 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. Computer applications to medicine. Medical informatics Science (General) Stefano Bruno verfasserin aut Luca Ronda verfasserin aut Gianluca Paredi verfasserin aut Stefano Bettati verfasserin aut Andrea Mozzarelli verfasserin aut In Data in Brief Elsevier, 2015 19(2018), Seite 2215-2220 (DE-627)797838937 (DE-600)2786545-9 23523409 nnns volume:19 year:2018 pages:2215-2220 https://doi.org/10.1016/j.dib.2018.06.088 kostenfrei https://doaj.org/article/a0876f37da15420095422e55b34e61e7 kostenfrei http://www.sciencedirect.com/science/article/pii/S235234091830739X kostenfrei https://doaj.org/toc/2352-3409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 19 2018 2215-2220 |
allfieldsGer |
10.1016/j.dib.2018.06.088 doi (DE-627)DOAJ075382814 (DE-599)DOAJa0876f37da15420095422e55b34e61e7 DE-627 ger DE-627 rakwb eng R858-859.7 Q1-390 Esra'a Alomari verfasserin aut Protein carbonylation detection methods: A comparison 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. Computer applications to medicine. Medical informatics Science (General) Stefano Bruno verfasserin aut Luca Ronda verfasserin aut Gianluca Paredi verfasserin aut Stefano Bettati verfasserin aut Andrea Mozzarelli verfasserin aut In Data in Brief Elsevier, 2015 19(2018), Seite 2215-2220 (DE-627)797838937 (DE-600)2786545-9 23523409 nnns volume:19 year:2018 pages:2215-2220 https://doi.org/10.1016/j.dib.2018.06.088 kostenfrei https://doaj.org/article/a0876f37da15420095422e55b34e61e7 kostenfrei http://www.sciencedirect.com/science/article/pii/S235234091830739X kostenfrei https://doaj.org/toc/2352-3409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 19 2018 2215-2220 |
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10.1016/j.dib.2018.06.088 doi (DE-627)DOAJ075382814 (DE-599)DOAJa0876f37da15420095422e55b34e61e7 DE-627 ger DE-627 rakwb eng R858-859.7 Q1-390 Esra'a Alomari verfasserin aut Protein carbonylation detection methods: A comparison 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. Computer applications to medicine. Medical informatics Science (General) Stefano Bruno verfasserin aut Luca Ronda verfasserin aut Gianluca Paredi verfasserin aut Stefano Bettati verfasserin aut Andrea Mozzarelli verfasserin aut In Data in Brief Elsevier, 2015 19(2018), Seite 2215-2220 (DE-627)797838937 (DE-600)2786545-9 23523409 nnns volume:19 year:2018 pages:2215-2220 https://doi.org/10.1016/j.dib.2018.06.088 kostenfrei https://doaj.org/article/a0876f37da15420095422e55b34e61e7 kostenfrei http://www.sciencedirect.com/science/article/pii/S235234091830739X kostenfrei https://doaj.org/toc/2352-3409 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 19 2018 2215-2220 |
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Esra'a Alomari @@aut@@ Stefano Bruno @@aut@@ Luca Ronda @@aut@@ Gianluca Paredi @@aut@@ Stefano Bettati @@aut@@ Andrea Mozzarelli @@aut@@ |
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R858-859.7 Q1-390 Protein carbonylation detection methods: A comparison |
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Protein carbonylation detection methods: A comparison |
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Protein carbonylation detection methods: A comparison |
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Esra'a Alomari Stefano Bruno Luca Ronda Gianluca Paredi Stefano Bettati Andrea Mozzarelli |
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protein carbonylation detection methods: a comparison |
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Protein carbonylation detection methods: A comparison |
abstract |
The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. |
abstractGer |
The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. |
abstract_unstemmed |
The data reported here are a comparison among four different methods for the detection of carbonylated proteins, a validated biomarker of oxidative stress. The reference samples were heart and kidney extracts of Guinea pigs transfused with hemoglobin-based oxygen carriers (Alomari et al. FRBM, [11]). We measured the carbonyl content of organ extracts by using i) the Levine spectrophotometric method, which takes advantage of the chromogenic reaction of carbonyl groups with 2,4-dinitrophenylhydrazine (DNPH), ii) a commercially available ELISA assay based on an anti-DNPH antibodies, iii) a commercially available Western blot method based on anti-DNPH antibodies and iv) an in-gel detection approach with the fluorophoric reagent fluorescein-5-thiosemicarbazide. The former two methods measure total protein carbonylation of a sample, whereas the latter two require an electrophoretic separation and therefore potentially allow for the identification of specific carbonylated proteins. |
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title_short |
Protein carbonylation detection methods: A comparison |
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https://doi.org/10.1016/j.dib.2018.06.088 https://doaj.org/article/a0876f37da15420095422e55b34e61e7 http://www.sciencedirect.com/science/article/pii/S235234091830739X https://doaj.org/toc/2352-3409 |
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