Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase
Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is ap...
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| Autor*in: |
Li, Zhen-Chang [verfasserIn] McClure, Jerry W. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1989 |
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| Schlagwörter: |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Physiologia plantarum - Oxford [u.a.] : Wiley-Blackwell, 1948, 77(1989), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:77 ; year:1989 ; number:3 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1111/j.1399-3054.1989.tb05652.x |
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| 245 | 1 | 0 | |a Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase |
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| 520 | |a Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. | ||
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10.1111/j.1399-3054.1989.tb05652.x doi (DE-627)NLEJ240957962 DE-627 ger DE-627 rakwb Li, Zhen-Chang verfasserin aut Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Apoplast McClure, Jerry W. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 77(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:77 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05652.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1989 3 0 |
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10.1111/j.1399-3054.1989.tb05652.x doi (DE-627)NLEJ240957962 DE-627 ger DE-627 rakwb Li, Zhen-Chang verfasserin aut Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Apoplast McClure, Jerry W. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 77(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:77 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05652.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1989 3 0 |
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10.1111/j.1399-3054.1989.tb05652.x doi (DE-627)NLEJ240957962 DE-627 ger DE-627 rakwb Li, Zhen-Chang verfasserin aut Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Apoplast McClure, Jerry W. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 77(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:77 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05652.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1989 3 0 |
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10.1111/j.1399-3054.1989.tb05652.x doi (DE-627)NLEJ240957962 DE-627 ger DE-627 rakwb Li, Zhen-Chang verfasserin aut Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Apoplast McClure, Jerry W. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 77(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:77 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05652.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1989 3 0 |
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10.1111/j.1399-3054.1989.tb05652.x doi (DE-627)NLEJ240957962 DE-627 ger DE-627 rakwb Li, Zhen-Chang verfasserin aut Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase Oxford, UK Blackwell Publishing Ltd 1989 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Apoplast McClure, Jerry W. verfasserin aut In Physiologia plantarum Oxford [u.a.] : Wiley-Blackwell, 1948 77(1989), 3, Seite 0 Online-Ressource (DE-627)NLEJ243927738 (DE-600)2020837-6 1399-3054 nnns volume:77 year:1989 number:3 pages:0 http://dx.doi.org/10.1111/j.1399-3054.1989.tb05652.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 77 1989 3 0 |
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Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase |
| abstract |
Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. |
| abstractGer |
Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. |
| abstract_unstemmed |
Mesophyll protoplasts isolated from peeled oat (Avena sativa L. cv Victory) leaves with 1% (w/v) Cellulysin in 20 mM KPO4, pH 5.5 and 0.6 M sorbitol retain about 6% of the polyamine oxidase (PAO, EC 1.4.3.4) activity of the whole peeled leaf. However, more than 99% of the oat leaf PAO activity is apoplastic and can be extracted by vacuum infiltration with 200 mM NaCl and this procedure extracts no activity for the cytoplasmic marker enzyme glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49). By these criteria we consider PAO in oat leaves to be totally apoplastic and PAO found in the isolated protoplast to be contamination. The degree of protoplast contamination by PAO depends on the pH and ionic strength of the isolating and washing medium. It can be eliminated by washing protoplasts in 0.6 M sorbitol with 100 mM KPO4, pH 6.5. Pellets of lysed protoplasts incubated with dialyzed apoplastic enzymes in 5 mM KPO4, pH 5.5 adsorb about 87% of the added PAO activity but only about 25% of the added peroxidase (EC 1.11.1.7) activity. The adsorbed activity can be solubilized from the pellet by extraction with 1 M NaCl. The results demonstrate that weakly ionically bound cell wall enzymes may contaminate protoplasts isolated and purified by conventional techniques. |
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Contamination of oat mesophyll protoplasts by apoplastic polyamine oxidase |
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