| Attributes | Values |
|---|
| rdf:type
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| Description
| - According to our knowledge, this is the first purification method developed, enabling isolation of a homogeneous aminoaldehyde dehydrogenase (AMADH) from etiolated pea seedlings. The procedure involved initial purification with precipitants followed by three low pressure chromatographic steps. Partially purified enzyme was further subjected to fast protein liquid chromatography on a Mono Q column and to affinity^interaction chromatography on 5P-AMP Sepharose. Purity of the final enzyme preparation was checked by sodium dodecyl sulfate^polyacrylamide gel electrophoresis and chromatofocusing. Pea AMADH exists as a tetramer of 230 kDa in the native state, a molecular mass of one subunit was determined as 57 kDa. The enzyme was found to be an acidic protein with pI 5.4. AMADH showed a broad substrate specificity utilising various aminoaldehydes (C3^C6) as substrates. The best substrate of pea AMADH was 3- aminopropionaldehyde, the enzyme also efficiently oxidised 4-aminobutyraldehyde and g-guanidinoanalog
- According to our knowledge, this is the first purification method developed, enabling isolation of a homogeneous aminoaldehyde dehydrogenase (AMADH) from etiolated pea seedlings. The procedure involved initial purification with precipitants followed by three low pressure chromatographic steps. Partially purified enzyme was further subjected to fast protein liquid chromatography on a Mono Q column and to affinity^interaction chromatography on 5P-AMP Sepharose. Purity of the final enzyme preparation was checked by sodium dodecyl sulfate^polyacrylamide gel electrophoresis and chromatofocusing. Pea AMADH exists as a tetramer of 230 kDa in the native state, a molecular mass of one subunit was determined as 57 kDa. The enzyme was found to be an acidic protein with pI 5.4. AMADH showed a broad substrate specificity utilising various aminoaldehydes (C3^C6) as substrates. The best substrate of pea AMADH was 3- aminopropionaldehyde, the enzyme also efficiently oxidised 4-aminobutyraldehyde and g-guanidinoanalog (en)
- According to our knowledge, this is the first purification method developed, enabling isolation of a homogeneous aminoaldehyde dehydrogenase (AMADH) from etiolated pea seedlings. The procedure involved initial purification with precipitants followed by three low pressure chromatographic steps. Partially purified enzyme was further subjected to fast protein liquid chromatography on a Mono Q column and to affinity^interaction chromatography on 5P-AMP Sepharose. Purity of the final enzyme preparation was checked by sodium dodecyl sulfate^polyacrylamide gel electrophoresis and chromatofocusing. Pea AMADH exists as a tetramer of 230 kDa in the native state, a molecular mass of one subunit was determined as 57 kDa. The enzyme was found to be an acidic protein with pI 5.4. AMADH showed a broad substrate specificity utilising various aminoaldehydes (C3^C6) as substrates. The best substrate of pea AMADH was 3- aminopropionaldehyde, the enzyme also efficiently oxidised 4-aminobutyraldehyde and g-guanidinoanalog (cs)
|
| Title
| - Characterisation of a homogenous plant aminoaldehyde dehydrogenase
- Characterisation of a homogenous plant aminoaldehyde dehydrogenase (en)
- Characterisation of a homogenous plant aminoaldehyde dehydrogenase (cs)
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| skos:prefLabel
| - Characterisation of a homogenous plant aminoaldehyde dehydrogenase
- Characterisation of a homogenous plant aminoaldehyde dehydrogenase (en)
- Characterisation of a homogenous plant aminoaldehyde dehydrogenase (cs)
|
| skos:notation
| - RIV/00216224:14310/00:00003346!RIV08-GA0-14310___
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| http://linked.open.../vavai/riv/strany
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
| |
| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/00216224:14310/00:00003346
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - aminoaldehyde dehydrogenase; 3-aminopropionaldehyde; 4-aminobutyraldehyde; pea; amine oxidase (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Biochimica et Biophysica Acta
|
| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Šebela, Marek
- Galuszka, Petr
- Havliš, Jan
- Peč, Pavel
|
| issn
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| number of pages
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| http://localhost/t...ganizacniJednotka
| |
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