$ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes
Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidatio...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Toyoda, Kazuhiro [verfasserIn] Yasunaga, Eri [verfasserIn] Niwa, Masanobu [verfasserIn] Ohwatari, Yuko [verfasserIn] Nakashima, Atsushi [verfasserIn] Inagaki, Yoshishige [verfasserIn] Ichinose, Yuki [verfasserIn] Shiraishi, Tomonori [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2012 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Journal of general plant pathology - Tokyo : Springer, 2000, 78(2012), 5 vom: 08. Aug., Seite 311-315 |
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| Übergeordnetes Werk: |
volume:78 ; year:2012 ; number:5 ; day:08 ; month:08 ; pages:311-315 |
| Links: |
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| DOI / URN: |
10.1007/s10327-012-0399-1 |
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| Katalog-ID: |
SPR009443045 |
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| 100 | 1 | |a Toyoda, Kazuhiro |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes |
| 264 | 1 | |c 2012 | |
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| 520 | |a Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. | ||
| 650 | 4 | |a Blue native PAGE |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Cell wall-associated ecto-apyrase (ATPase) |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Copper amine oxidase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Pea ( |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a L.) |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Suppressor |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Yasunaga, Eri |e verfasserin |4 aut | |
| 700 | 1 | |a Niwa, Masanobu |e verfasserin |4 aut | |
| 700 | 1 | |a Ohwatari, Yuko |e verfasserin |4 aut | |
| 700 | 1 | |a Nakashima, Atsushi |e verfasserin |4 aut | |
| 700 | 1 | |a Inagaki, Yoshishige |e verfasserin |4 aut | |
| 700 | 1 | |a Ichinose, Yuki |e verfasserin |4 aut | |
| 700 | 1 | |a Shiraishi, Tomonori |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Journal of general plant pathology |d Tokyo : Springer, 2000 |g 78(2012), 5 vom: 08. Aug., Seite 311-315 |w (DE-627)362771189 |w (DE-600)2100156-X |x 1610-739X |7 nnns |
| 773 | 1 | 8 | |g volume:78 |g year:2012 |g number:5 |g day:08 |g month:08 |g pages:311-315 |
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10.1007/s10327-012-0399-1 doi (DE-627)SPR009443045 (SPR)s10327-012-0399-1-e DE-627 ger DE-627 rakwb eng 630 ASE 580 ASE 48.54 bkl Toyoda, Kazuhiro verfasserin aut $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. Blue native PAGE (dpeaa)DE-He213 Cell wall-associated ecto-apyrase (ATPase) (dpeaa)DE-He213 Copper amine oxidase (dpeaa)DE-He213 Pea ( (dpeaa)DE-He213 L.) (dpeaa)DE-He213 Suppressor (dpeaa)DE-He213 Yasunaga, Eri verfasserin aut Niwa, Masanobu verfasserin aut Ohwatari, Yuko verfasserin aut Nakashima, Atsushi verfasserin aut Inagaki, Yoshishige verfasserin aut Ichinose, Yuki verfasserin aut Shiraishi, Tomonori verfasserin aut Enthalten in Journal of general plant pathology Tokyo : Springer, 2000 78(2012), 5 vom: 08. Aug., Seite 311-315 (DE-627)362771189 (DE-600)2100156-X 1610-739X nnns volume:78 year:2012 number:5 day:08 month:08 pages:311-315 https://dx.doi.org/10.1007/s10327-012-0399-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 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_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 48.54 ASE AR 78 2012 5 08 08 311-315 |
| spelling |
10.1007/s10327-012-0399-1 doi (DE-627)SPR009443045 (SPR)s10327-012-0399-1-e DE-627 ger DE-627 rakwb eng 630 ASE 580 ASE 48.54 bkl Toyoda, Kazuhiro verfasserin aut $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. Blue native PAGE (dpeaa)DE-He213 Cell wall-associated ecto-apyrase (ATPase) (dpeaa)DE-He213 Copper amine oxidase (dpeaa)DE-He213 Pea ( (dpeaa)DE-He213 L.) (dpeaa)DE-He213 Suppressor (dpeaa)DE-He213 Yasunaga, Eri verfasserin aut Niwa, Masanobu verfasserin aut Ohwatari, Yuko verfasserin aut Nakashima, Atsushi verfasserin aut Inagaki, Yoshishige verfasserin aut Ichinose, Yuki verfasserin aut Shiraishi, Tomonori verfasserin aut Enthalten in Journal of general plant pathology Tokyo : Springer, 2000 78(2012), 5 vom: 08. Aug., Seite 311-315 (DE-627)362771189 (DE-600)2100156-X 1610-739X nnns volume:78 year:2012 number:5 day:08 month:08 pages:311-315 https://dx.doi.org/10.1007/s10327-012-0399-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 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_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 48.54 ASE AR 78 2012 5 08 08 311-315 |
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10.1007/s10327-012-0399-1 doi (DE-627)SPR009443045 (SPR)s10327-012-0399-1-e DE-627 ger DE-627 rakwb eng 630 ASE 580 ASE 48.54 bkl Toyoda, Kazuhiro verfasserin aut $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. Blue native PAGE (dpeaa)DE-He213 Cell wall-associated ecto-apyrase (ATPase) (dpeaa)DE-He213 Copper amine oxidase (dpeaa)DE-He213 Pea ( (dpeaa)DE-He213 L.) (dpeaa)DE-He213 Suppressor (dpeaa)DE-He213 Yasunaga, Eri verfasserin aut Niwa, Masanobu verfasserin aut Ohwatari, Yuko verfasserin aut Nakashima, Atsushi verfasserin aut Inagaki, Yoshishige verfasserin aut Ichinose, Yuki verfasserin aut Shiraishi, Tomonori verfasserin aut Enthalten in Journal of general plant pathology Tokyo : Springer, 2000 78(2012), 5 vom: 08. Aug., Seite 311-315 (DE-627)362771189 (DE-600)2100156-X 1610-739X nnns volume:78 year:2012 number:5 day:08 month:08 pages:311-315 https://dx.doi.org/10.1007/s10327-012-0399-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 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_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 48.54 ASE AR 78 2012 5 08 08 311-315 |
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10.1007/s10327-012-0399-1 doi (DE-627)SPR009443045 (SPR)s10327-012-0399-1-e DE-627 ger DE-627 rakwb eng 630 ASE 580 ASE 48.54 bkl Toyoda, Kazuhiro verfasserin aut $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. Blue native PAGE (dpeaa)DE-He213 Cell wall-associated ecto-apyrase (ATPase) (dpeaa)DE-He213 Copper amine oxidase (dpeaa)DE-He213 Pea ( (dpeaa)DE-He213 L.) (dpeaa)DE-He213 Suppressor (dpeaa)DE-He213 Yasunaga, Eri verfasserin aut Niwa, Masanobu verfasserin aut Ohwatari, Yuko verfasserin aut Nakashima, Atsushi verfasserin aut Inagaki, Yoshishige verfasserin aut Ichinose, Yuki verfasserin aut Shiraishi, Tomonori verfasserin aut Enthalten in Journal of general plant pathology Tokyo : Springer, 2000 78(2012), 5 vom: 08. Aug., Seite 311-315 (DE-627)362771189 (DE-600)2100156-X 1610-739X nnns volume:78 year:2012 number:5 day:08 month:08 pages:311-315 https://dx.doi.org/10.1007/s10327-012-0399-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 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_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 48.54 ASE AR 78 2012 5 08 08 311-315 |
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10.1007/s10327-012-0399-1 doi (DE-627)SPR009443045 (SPR)s10327-012-0399-1-e DE-627 ger DE-627 rakwb eng 630 ASE 580 ASE 48.54 bkl Toyoda, Kazuhiro verfasserin aut $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes 2012 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. Blue native PAGE (dpeaa)DE-He213 Cell wall-associated ecto-apyrase (ATPase) (dpeaa)DE-He213 Copper amine oxidase (dpeaa)DE-He213 Pea ( (dpeaa)DE-He213 L.) (dpeaa)DE-He213 Suppressor (dpeaa)DE-He213 Yasunaga, Eri verfasserin aut Niwa, Masanobu verfasserin aut Ohwatari, Yuko verfasserin aut Nakashima, Atsushi verfasserin aut Inagaki, Yoshishige verfasserin aut Ichinose, Yuki verfasserin aut Shiraishi, Tomonori verfasserin aut Enthalten in Journal of general plant pathology Tokyo : Springer, 2000 78(2012), 5 vom: 08. Aug., Seite 311-315 (DE-627)362771189 (DE-600)2100156-X 1610-739X nnns volume:78 year:2012 number:5 day:08 month:08 pages:311-315 https://dx.doi.org/10.1007/s10327-012-0399-1 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 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_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_267 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 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_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 48.54 ASE AR 78 2012 5 08 08 311-315 |
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English |
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Enthalten in Journal of general plant pathology 78(2012), 5 vom: 08. Aug., Seite 311-315 volume:78 year:2012 number:5 day:08 month:08 pages:311-315 |
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Enthalten in Journal of general plant pathology 78(2012), 5 vom: 08. Aug., Seite 311-315 volume:78 year:2012 number:5 day:08 month:08 pages:311-315 |
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findex.gbv.de |
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Blue native PAGE Cell wall-associated ecto-apyrase (ATPase) Copper amine oxidase Pea ( L.) Suppressor |
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Journal of general plant pathology |
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Toyoda, Kazuhiro @@aut@@ Yasunaga, Eri @@aut@@ Niwa, Masanobu @@aut@@ Ohwatari, Yuko @@aut@@ Nakashima, Atsushi @@aut@@ Inagaki, Yoshishige @@aut@@ Ichinose, Yuki @@aut@@ Shiraishi, Tomonori @@aut@@ |
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2012-08-08T00:00:00Z |
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CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. 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| author |
Toyoda, Kazuhiro |
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Toyoda, Kazuhiro ddc 630 ddc 580 bkl 48.54 misc Blue native PAGE misc Cell wall-associated ecto-apyrase (ATPase) misc Copper amine oxidase misc Pea ( misc L.) misc Suppressor $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes |
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630 ASE 580 ASE 48.54 bkl $ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes Blue native PAGE (dpeaa)DE-He213 Cell wall-associated ecto-apyrase (ATPase) (dpeaa)DE-He213 Copper amine oxidase (dpeaa)DE-He213 Pea ( (dpeaa)DE-He213 L.) (dpeaa)DE-He213 Suppressor (dpeaa)DE-He213 |
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ddc 630 ddc 580 bkl 48.54 misc Blue native PAGE misc Cell wall-associated ecto-apyrase (ATPase) misc Copper amine oxidase misc Pea ( misc L.) misc Suppressor |
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ddc 630 ddc 580 bkl 48.54 misc Blue native PAGE misc Cell wall-associated ecto-apyrase (ATPase) misc Copper amine oxidase misc Pea ( misc L.) misc Suppressor |
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$ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes |
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| title_full |
$ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes |
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Toyoda, Kazuhiro |
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Journal of general plant pathology |
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Journal of general plant pathology |
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eng |
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600 - Technology 500 - Science |
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2012 |
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Toyoda, Kazuhiro Yasunaga, Eri Niwa, Masanobu Ohwatari, Yuko Nakashima, Atsushi Inagaki, Yoshishige Ichinose, Yuki Shiraishi, Tomonori |
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Elektronische Aufsätze |
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Toyoda, Kazuhiro |
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10.1007/s10327-012-0399-1 |
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630 580 |
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verfasserin |
| title_sort |
$ h_{2} %$ o_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (atpase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from mycosphaerella pinodes |
| title_auth |
$ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes |
| abstract |
Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. |
| abstractGer |
Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. |
| abstract_unstemmed |
Abstract Blue native PAGE analysis for cell wall proteins from pea epicotyls demonstrated that cell wall-associated ecto-apyrase (ATPase) formed a large protein complex(es) ranging from 450 to 900 kDa; one of the components of the complex was copper amine oxidase (CuAO), which catalyzes the oxidation of amines with the subsequent generation of ammonia and hydrogen peroxide. CuAO activity was coordinately regulated in vitro with ATP-hydrolyzing activity by an elicitor and a suppressor from Mycosphaerella pinodes. Moreover, treatment of cell wall proteins with the suppressor caused the appearance of the apyrase monomer. On the basis of these results, M. pinodes may target the apyrase-containing protein complex(es) of the host to attenuate cell wall-based, extracellular defense(s) including the production of hydrogen peroxide. |
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| title_short |
$ H_{2} %$ O_{2} $ production by copper amine oxidase, a component of the ecto-apyrase (ATPase)-containing protein complex(es) in the pea cell wall, is regulated by an elicitor and a suppressor from Mycosphaerella pinodes |
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Yasunaga, Eri Niwa, Masanobu Ohwatari, Yuko Nakashima, Atsushi Inagaki, Yoshishige Ichinose, Yuki Shiraishi, Tomonori |
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Yasunaga, Eri Niwa, Masanobu Ohwatari, Yuko Nakashima, Atsushi Inagaki, Yoshishige Ichinose, Yuki Shiraishi, Tomonori |
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| score |
7.401205 |