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OtherMETABOLISM AND ENZYMOLOGY
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An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts

T. Koshiba, H. Matsuyama
T. Koshiba
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H. Matsuyama
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Published August 1993. DOI: https://doi.org/10.1104/pp.102.4.1319

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Abstract

The formation of a product from tryptophan that had the same retention time as that of authentic indole-3-acetic acid (IAA) on high performance liquid chromatography was detected in crude extracts of maize (Zea mays) coleoptiles. The product was identified as IAA by mass spectrometry. The IAA-forming activity was co-purified with an indole-3-acetaldehyde (IAAld) oxidase activity by chromatography on hydrophobic and gel filtration (GPC-100) columns. During purification, the IAA-forming activity, rather than that of IAAld oxidase, decreased; but when hemoprotein obtained from the same tissue was added, activity recovered to the same level as that of IAAld oxidase. The promotive activity of the hemoprotein was confirmed by the result that the activity coincided with amounts of the hemoprotein after GPC-100 column chromatography. The hemoprotein was characterized and identified as a cytosolic ascorbate peroxidase (T. Koshiba [1993] Plant Cell Physiol [in press]). The reaction of the IAA-forming activity was apparently one step from tryptophan. The activity was inhibited by 2-mercaptoethanol. The optimum temperature for the IAA-forming system as well as for the IAAld oxidase was 50 to 60[deg]C, and the acitivity at 30[deg]C was one-third to one-half of that at 60[deg]C. The system did not discriminate the L- and D-enantiomers of tryptophan.

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An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts
T. Koshiba, H. Matsuyama
Plant Physiology Aug 1993, 102 (4) 1319-1324; DOI: 10.1104/pp.102.4.1319

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An in Vitro System of Indole-3-Acetic Acid Formation from Tryptophan in Maize (Zea mays) Coleoptile Extracts
T. Koshiba, H. Matsuyama
Plant Physiology Aug 1993, 102 (4) 1319-1324; DOI: 10.1104/pp.102.4.1319
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Plant Physiology
Vol. 102, Issue 4
Aug 1993
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  • Identification of Posttranslationally Modified 18-Kilodalton Protein from Rice as Eukaryotic Translation Initiation Factor 5A
  • Regulation of Maize Leaf Nitrate Reductase Activity Involves Both Gene Expression and Protein Phosphorylation
  • Inhibition of Barnyardgrass 4-Hydroxyphenylpyruvate Dioxygenase by Sulcotrione
Show more Metabolism and Enzymology

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