Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro
Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific...
Ausführliche Beschreibung
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| Autor*in: |
Purohit, Jogeswar S. [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: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation - Duan, Cong ELSEVIER, 2022, an international journal of biochemistry and molecular biology, Paris [u.a.] |
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| Übergeordnetes Werk: |
volume:95 ; year:2013 ; number:11 ; pages:1999-2009 ; extent:11 |
| Links: |
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| DOI / URN: |
10.1016/j.biochi.2013.07.005 |
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| 245 | 1 | 0 | |a Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro |
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| 520 | |a Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. | ||
| 520 | |a Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. | ||
| 650 | 7 | |a Histone H3-specific protease |2 Elsevier | |
| 650 | 7 | |a Moonlighting protease |2 Elsevier | |
| 650 | 7 | |a H3ase |2 Elsevier | |
| 650 | 7 | |a Glutamate dehydrogenase (GDH) |2 Elsevier | |
| 650 | 7 | |a Irreversible modification of histone H3 |2 Elsevier | |
| 650 | 7 | |a Histone H3 proteolysis |2 Elsevier | |
| 700 | 1 | |a Tomar, Raghuvir S. |4 oth | |
| 700 | 1 | |a Panigrahi, Anil K. |4 oth | |
| 700 | 1 | |a Pandey, Shashibhal M. |4 oth | |
| 700 | 1 | |a Singh, Divya |4 oth | |
| 700 | 1 | |a Chaturvedi, Madan M. |4 oth | |
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10.1016/j.biochi.2013.07.005 doi GBVA2013009000019.pica (DE-627)ELV021844534 (ELSEVIER)S0300-9084(13)00214-9 DE-627 ger DE-627 rakwb eng 540 540 DE-600 600 VZ 50.70 bkl Purohit, Jogeswar S. verfasserin aut Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro 2013transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Histone H3-specific protease Elsevier Moonlighting protease Elsevier H3ase Elsevier Glutamate dehydrogenase (GDH) Elsevier Irreversible modification of histone H3 Elsevier Histone H3 proteolysis Elsevier Tomar, Raghuvir S. oth Panigrahi, Anil K. oth Pandey, Shashibhal M. oth Singh, Divya oth Chaturvedi, Madan M. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:95 year:2013 number:11 pages:1999-2009 extent:11 https://doi.org/10.1016/j.biochi.2013.07.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 95 2013 11 1999-2009 11 045F 540 |
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10.1016/j.biochi.2013.07.005 doi GBVA2013009000019.pica (DE-627)ELV021844534 (ELSEVIER)S0300-9084(13)00214-9 DE-627 ger DE-627 rakwb eng 540 540 DE-600 600 VZ 50.70 bkl Purohit, Jogeswar S. verfasserin aut Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro 2013transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Histone H3-specific protease Elsevier Moonlighting protease Elsevier H3ase Elsevier Glutamate dehydrogenase (GDH) Elsevier Irreversible modification of histone H3 Elsevier Histone H3 proteolysis Elsevier Tomar, Raghuvir S. oth Panigrahi, Anil K. oth Pandey, Shashibhal M. oth Singh, Divya oth Chaturvedi, Madan M. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:95 year:2013 number:11 pages:1999-2009 extent:11 https://doi.org/10.1016/j.biochi.2013.07.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 95 2013 11 1999-2009 11 045F 540 |
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10.1016/j.biochi.2013.07.005 doi GBVA2013009000019.pica (DE-627)ELV021844534 (ELSEVIER)S0300-9084(13)00214-9 DE-627 ger DE-627 rakwb eng 540 540 DE-600 600 VZ 50.70 bkl Purohit, Jogeswar S. verfasserin aut Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro 2013transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Histone H3-specific protease Elsevier Moonlighting protease Elsevier H3ase Elsevier Glutamate dehydrogenase (GDH) Elsevier Irreversible modification of histone H3 Elsevier Histone H3 proteolysis Elsevier Tomar, Raghuvir S. oth Panigrahi, Anil K. oth Pandey, Shashibhal M. oth Singh, Divya oth Chaturvedi, Madan M. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:95 year:2013 number:11 pages:1999-2009 extent:11 https://doi.org/10.1016/j.biochi.2013.07.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 95 2013 11 1999-2009 11 045F 540 |
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10.1016/j.biochi.2013.07.005 doi GBVA2013009000019.pica (DE-627)ELV021844534 (ELSEVIER)S0300-9084(13)00214-9 DE-627 ger DE-627 rakwb eng 540 540 DE-600 600 VZ 50.70 bkl Purohit, Jogeswar S. verfasserin aut Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro 2013transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Histone H3-specific protease Elsevier Moonlighting protease Elsevier H3ase Elsevier Glutamate dehydrogenase (GDH) Elsevier Irreversible modification of histone H3 Elsevier Histone H3 proteolysis Elsevier Tomar, Raghuvir S. oth Panigrahi, Anil K. oth Pandey, Shashibhal M. oth Singh, Divya oth Chaturvedi, Madan M. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:95 year:2013 number:11 pages:1999-2009 extent:11 https://doi.org/10.1016/j.biochi.2013.07.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 95 2013 11 1999-2009 11 045F 540 |
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10.1016/j.biochi.2013.07.005 doi GBVA2013009000019.pica (DE-627)ELV021844534 (ELSEVIER)S0300-9084(13)00214-9 DE-627 ger DE-627 rakwb eng 540 540 DE-600 600 VZ 50.70 bkl Purohit, Jogeswar S. verfasserin aut Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro 2013transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. Histone H3-specific protease Elsevier Moonlighting protease Elsevier H3ase Elsevier Glutamate dehydrogenase (GDH) Elsevier Irreversible modification of histone H3 Elsevier Histone H3 proteolysis Elsevier Tomar, Raghuvir S. oth Panigrahi, Anil K. oth Pandey, Shashibhal M. oth Singh, Divya oth Chaturvedi, Madan M. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:95 year:2013 number:11 pages:1999-2009 extent:11 https://doi.org/10.1016/j.biochi.2013.07.005 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 95 2013 11 1999-2009 11 045F 540 |
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Enthalten in Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation Paris [u.a.] volume:95 year:2013 number:11 pages:1999-2009 extent:11 |
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Enthalten in Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation Paris [u.a.] volume:95 year:2013 number:11 pages:1999-2009 extent:11 |
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Histone H3-specific protease Moonlighting protease H3ase Glutamate dehydrogenase (GDH) Irreversible modification of histone H3 Histone H3 proteolysis |
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Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation |
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Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro |
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Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. |
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Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. |
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Site-specific proteolysis of the N or C-terminus of histone tails has emerged as a novel form of irreversible post-translational modifications assigned to histones. Though there are many reports describing histone specific proteolysis, there are very few studies on purification of a histone specific protease. Here, we demonstrate a histone H3 specific protease (H3ase) activity in chicken liver nuclear extract. H3ase was purified to homogeneity and identified as glutamate dehydrogenase (GDH) by sequencing. A series of biochemical experiments further confirmed that the H3ase activity was due to GDH. The H3ase clipped histone H3 products were sequenced by N-terminal sequencing and the precise clipping sites of H3ase were mapped. H3ase activity was only specific to chicken liver as it was not demonstrated in other tissues like heart, muscle and brain of chicken. We assign a novel serine like protease activity to GDH which is specific to histone H3. |
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