Adenyiyl Cyclase and G-Proteins in Phytomonas
. Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activit...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
FARBER, MARISA D. [verfasserIn] MONTAGNA, ANDREA E. [verfasserIn] PAVETO, CRISTINA [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1995 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2007 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: The journal of eukaryotic microbiology - Oxford [u.a.] : Wiley-Blackwell, 1954, 42(1995), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:42 ; year:1995 ; number:3 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1550-7408.1995.tb01576.x |
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| 520 | |a . Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. | ||
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10.1111/j.1550-7408.1995.tb01576.x doi (DE-627)NLEJ240633458 DE-627 ger DE-627 rakwb FARBER, MARISA D. verfasserin aut Adenyiyl Cyclase and G-Proteins in Phytomonas Oxford, UK Blackwell Publishing Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier . Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| ADP-ribosylation MONTAGNA, ANDREA E. verfasserin aut PAVETO, CRISTINA verfasserin aut DOLLET, MICHEL oth SANCHEZ-MORENO, MANUEL oth OSUNA, ANTONIO oth TORRES, HECTOR N. oth FLAWIA, MIRTHA M. oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 42(1995), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:42 year:1995 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1995.tb01576.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 42 1995 3 0 |
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10.1111/j.1550-7408.1995.tb01576.x doi (DE-627)NLEJ240633458 DE-627 ger DE-627 rakwb FARBER, MARISA D. verfasserin aut Adenyiyl Cyclase and G-Proteins in Phytomonas Oxford, UK Blackwell Publishing Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier . Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| ADP-ribosylation MONTAGNA, ANDREA E. verfasserin aut PAVETO, CRISTINA verfasserin aut DOLLET, MICHEL oth SANCHEZ-MORENO, MANUEL oth OSUNA, ANTONIO oth TORRES, HECTOR N. oth FLAWIA, MIRTHA M. oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 42(1995), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:42 year:1995 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1995.tb01576.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 42 1995 3 0 |
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10.1111/j.1550-7408.1995.tb01576.x doi (DE-627)NLEJ240633458 DE-627 ger DE-627 rakwb FARBER, MARISA D. verfasserin aut Adenyiyl Cyclase and G-Proteins in Phytomonas Oxford, UK Blackwell Publishing Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier . Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| ADP-ribosylation MONTAGNA, ANDREA E. verfasserin aut PAVETO, CRISTINA verfasserin aut DOLLET, MICHEL oth SANCHEZ-MORENO, MANUEL oth OSUNA, ANTONIO oth TORRES, HECTOR N. oth FLAWIA, MIRTHA M. oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 42(1995), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:42 year:1995 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1995.tb01576.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 42 1995 3 0 |
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10.1111/j.1550-7408.1995.tb01576.x doi (DE-627)NLEJ240633458 DE-627 ger DE-627 rakwb FARBER, MARISA D. verfasserin aut Adenyiyl Cyclase and G-Proteins in Phytomonas Oxford, UK Blackwell Publishing Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier . Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| ADP-ribosylation MONTAGNA, ANDREA E. verfasserin aut PAVETO, CRISTINA verfasserin aut DOLLET, MICHEL oth SANCHEZ-MORENO, MANUEL oth OSUNA, ANTONIO oth TORRES, HECTOR N. oth FLAWIA, MIRTHA M. oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 42(1995), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:42 year:1995 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1995.tb01576.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 42 1995 3 0 |
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10.1111/j.1550-7408.1995.tb01576.x doi (DE-627)NLEJ240633458 DE-627 ger DE-627 rakwb FARBER, MARISA D. verfasserin aut Adenyiyl Cyclase and G-Proteins in Phytomonas Oxford, UK Blackwell Publishing Ltd 1995 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier . Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. 2007 Blackwell Publishing Journal Backfiles 1879-2005 |2007|||||||||| ADP-ribosylation MONTAGNA, ANDREA E. verfasserin aut PAVETO, CRISTINA verfasserin aut DOLLET, MICHEL oth SANCHEZ-MORENO, MANUEL oth OSUNA, ANTONIO oth TORRES, HECTOR N. oth FLAWIA, MIRTHA M. oth In The journal of eukaryotic microbiology Oxford [u.a.] : Wiley-Blackwell, 1954 42(1995), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927622 (DE-600)2126326-7 1550-7408 nnns volume:42 year:1995 number:3 pages:0 http://dx.doi.org/10.1111/j.1550-7408.1995.tb01576.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 42 1995 3 0 |
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Adenyiyl Cyclase and G-Proteins in Phytomonas |
| abstract |
. Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. |
| abstractGer |
. Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. |
| abstract_unstemmed |
. Phytomonas sp. membranes have an adenylyl cyclase activity which is greater in the presence of Mn2+ than with Mg2+. The Mg2+ and Mn2+ activity ratio varies from one membrane preparation to another, suggesting that the adenylyl cyclase has a variable activation state. A [35S]GTP-γ-S-binding activity with a Kd of 171 nM was detected in Phytomonas membranes. Incubation of these membranes with activated cholera or pertussis toxin and [adenylate 32P]NAD+ led to incorporation of radioactivity into bands of about 40–44 kDa. Crude membranes were electrophoresed on SDS-polyacrylamide gels and analyzed, by Western blotting, with the 9188 anti-αs antibody and the AS/7 antibody (anti-α1, anti-αi1, anti-αi2). These procedures resulted in the identification of polypeptides of approximately 40–44 kDa. Phytomonas adenylyl cyclase could be activated by treatment of membrane preparations with cholera toxin, in the presence of NAD+, while similar treatment with pertussis toxin did not affect this enzyme activity. These studies indicate that in Phytomonas, adenylyl cyclase activity is coupled to an unknown receptor entity through Gαs, proteins. |
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| title_short |
Adenyiyl Cyclase and G-Proteins in Phytomonas |
| url |
http://dx.doi.org/10.1111/j.1550-7408.1995.tb01576.x |
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| author2 |
MONTAGNA, ANDREA E. PAVETO, CRISTINA DOLLET, MICHEL SANCHEZ-MORENO, MANUEL OSUNA, ANTONIO TORRES, HECTOR N. FLAWIA, MIRTHA M. |
| author2Str |
MONTAGNA, ANDREA E. PAVETO, CRISTINA DOLLET, MICHEL SANCHEZ-MORENO, MANUEL OSUNA, ANTONIO TORRES, HECTOR N. FLAWIA, MIRTHA M. |
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| doi_str |
10.1111/j.1550-7408.1995.tb01576.x |
| up_date |
2024-07-06T10:30:28.679Z |
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7.3990517 |