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DE-627 |
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20231223044853.0 |
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231223s2004 xx ||||| 00| ||eng c |
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|a pubmed24n0494.xml
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|a (DE-627)NLM148115314
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|a (NLM)15120115
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Ha, Byung Hak
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Characterization of arginine decarboxylase from Dianthus caryophyllus
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| 264 |
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|c 2004
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 08.07.2004
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|a Date Revised 30.09.2020
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|a published: Print
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|a Citation Status MEDLINE
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|a Arginine decarboxylase (ADC, EC 4.1.1.9) is a key enzyme in the biosynthesis of polyamines in higher plants, whereas ornithine decarboxylase represents the sole pathway of polyamine biosynthesis in animals. Previously, we characterized a genomic clone from Dianthus caryophyllus, in which the deduced polypeptide of ADC was 725 amino acids with a molecular mass of 78 kDa. In the present study, the ADC gene was subcloned into the pGEX4T1 expression vector in combination with glutathione S-transferase (GST). The fusion protein GST-ADC was water-soluble and thus was purified by sequential GSTrap-arginine affinity chromatography. A thrombin-mediated on-column cleavage reaction was employed to release free ADC from GST. Hiload superdex gel filtration FPLC was then used to obtain a highly purified ADC. The identity of the ADC was confirmed by immunoblot analysis, and its specific activity with respect to (14)C-arginine decarboxylation reaction was determined to be 0.9 CO(2) pkat mg(-1) protein. K(m) and V(max) of the reaction between ADC and the substrate were 0.077 +/- 0.001 mM and 6.0 +/- 0.6 pkat mg(-1) protein, respectively. ADC activity was reduced by 70% in the presence of 0.1 mM Cu(2+) or CO(2+), but was only marginally affected by Mg(2+), or Ca(2+) at the same concentration. Moreover, spermine at 1 mM significantly reduced its activity by 30%
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Enzyme Inhibitors
|2 NLM
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|a Metals, Heavy
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a Recombinant Fusion Proteins
|2 NLM
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| 650 |
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|a Spermine
|2 NLM
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| 650 |
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7 |
|a 2FZ7Y3VOQX
|2 NLM
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| 650 |
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|a Carboxy-Lyases
|2 NLM
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| 650 |
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|a EC 4.1.1.-
|2 NLM
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| 650 |
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|a arginine decarboxylase
|2 NLM
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| 650 |
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|a EC 4.1.1.19
|2 NLM
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| 650 |
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|a Magnesium
|2 NLM
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| 650 |
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|a I38ZP9992A
|2 NLM
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| 650 |
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|a Calcium
|2 NLM
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| 650 |
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7 |
|a SY7Q814VUP
|2 NLM
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| 650 |
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7 |
|a Spermidine
|2 NLM
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| 650 |
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|a U87FK77H25
|2 NLM
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| 650 |
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|a Putrescine
|2 NLM
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| 650 |
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|a V10TVZ52E4
|2 NLM
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| 700 |
1 |
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|a Cho, Ki Joon
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Choi, Yu Jin
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Park, Ky Young
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Kim, Kyung Hyun
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Plant physiology and biochemistry : PPB
|d 1991
|g 42(2004), 4 vom: 04. Apr., Seite 307-11
|w (DE-627)NLM098178261
|x 1873-2690
|7 nnns
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| 773 |
1 |
8 |
|g volume:42
|g year:2004
|g number:4
|g day:04
|g month:04
|g pages:307-11
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_350
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|a AR
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| 952 |
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|d 42
|j 2004
|e 4
|b 04
|c 04
|h 307-11
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