A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide
The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Tripathy, Debi Ranjan [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2013transfer abstract |
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| Schlagwörter: |
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| Umfang: |
4 |
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| Übergeordnetes Werk: |
Enthalten in: Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems - Kroon, Frederieke J. ELSEVIER, 2014, methods in the biological sciences, San Diego, Calif |
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| Übergeordnetes Werk: |
volume:437 ; year:2013 ; number:2 ; day:15 ; month:06 ; pages:126-129 ; extent:4 |
| Links: |
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| DOI / URN: |
10.1016/j.ab.2013.03.005 |
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ELV033462089 |
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| 520 | |a The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. | ||
| 520 | |a The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. | ||
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10.1016/j.ab.2013.03.005 doi GBVA2013019000023.pica (DE-627)ELV033462089 (ELSEVIER)S0003-2697(13)00124-3 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Tripathy, Debi Ranjan verfasserin aut A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide 2013transfer abstract 4 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. Ribonuclease A Elsevier Ethidium bromide Elsevier Ribonucleic acid Elsevier Ribonucleolytic assay Elsevier Angiogenin Elsevier Dinda, Amit Kumar oth Dasgupta, Swagata oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 https://doi.org/10.1016/j.ab.2013.03.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 437 2013 2 15 0615 126-129 4 045F 570 |
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10.1016/j.ab.2013.03.005 doi GBVA2013019000023.pica (DE-627)ELV033462089 (ELSEVIER)S0003-2697(13)00124-3 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Tripathy, Debi Ranjan verfasserin aut A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide 2013transfer abstract 4 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. Ribonuclease A Elsevier Ethidium bromide Elsevier Ribonucleic acid Elsevier Ribonucleolytic assay Elsevier Angiogenin Elsevier Dinda, Amit Kumar oth Dasgupta, Swagata oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 https://doi.org/10.1016/j.ab.2013.03.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 437 2013 2 15 0615 126-129 4 045F 570 |
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10.1016/j.ab.2013.03.005 doi GBVA2013019000023.pica (DE-627)ELV033462089 (ELSEVIER)S0003-2697(13)00124-3 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Tripathy, Debi Ranjan verfasserin aut A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide 2013transfer abstract 4 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. Ribonuclease A Elsevier Ethidium bromide Elsevier Ribonucleic acid Elsevier Ribonucleolytic assay Elsevier Angiogenin Elsevier Dinda, Amit Kumar oth Dasgupta, Swagata oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 https://doi.org/10.1016/j.ab.2013.03.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 437 2013 2 15 0615 126-129 4 045F 570 |
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10.1016/j.ab.2013.03.005 doi GBVA2013019000023.pica (DE-627)ELV033462089 (ELSEVIER)S0003-2697(13)00124-3 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Tripathy, Debi Ranjan verfasserin aut A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide 2013transfer abstract 4 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. Ribonuclease A Elsevier Ethidium bromide Elsevier Ribonucleic acid Elsevier Ribonucleolytic assay Elsevier Angiogenin Elsevier Dinda, Amit Kumar oth Dasgupta, Swagata oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 https://doi.org/10.1016/j.ab.2013.03.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 437 2013 2 15 0615 126-129 4 045F 570 |
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10.1016/j.ab.2013.03.005 doi GBVA2013019000023.pica (DE-627)ELV033462089 (ELSEVIER)S0003-2697(13)00124-3 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Tripathy, Debi Ranjan verfasserin aut A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide 2013transfer abstract 4 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. Ribonuclease A Elsevier Ethidium bromide Elsevier Ribonucleic acid Elsevier Ribonucleolytic assay Elsevier Angiogenin Elsevier Dinda, Amit Kumar oth Dasgupta, Swagata oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 https://doi.org/10.1016/j.ab.2013.03.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 437 2013 2 15 0615 126-129 4 045F 570 |
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Enthalten in Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems San Diego, Calif volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 |
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Enthalten in Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems San Diego, Calif volume:437 year:2013 number:2 day:15 month:06 pages:126-129 extent:4 |
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Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems |
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a simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide |
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A simple assay for the ribonuclease activity of ribonucleases in the presence of ethidium bromide |
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The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. |
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The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. |
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The ribonuclease (RNase) activity of ribonucleases has been assayed by observing the change in fluorescence intensity of ethidium bromide on binding with yeast RNA. The binding of EtBr with RNA was monitored via UV–vis and fluorimetric methods. The degradation of RNA by RNase A was monitored by the change in fluorescence emission intensity of ethidium bromide at 600nm on excitation at 510nm. The ribonucleolytic activity of RNase A and angiogenin at various pH values was determined by this method. From this technique we have also determined the macroscopic pK a values of active site residues of these enzymes. This assay permits the evaluation of the catalytic efficiency of enzymatic proteins ranging from high ribonucleolytic activity to low ribonucleolytic activity toward the natural substrate RNA. |
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