AN IN-VITRO SYSTEM OF INDOLE-3-ACETIC-ACID FORMATION FROM TRYPTOPHAN IN MAIZE (ZEA-MAYS) COLEOPTILE EXTRACTS

被引:42
作者
KOSHIBA, T [1 ]
MATSUYAMA, H [1 ]
机构
[1] TOKYO METROPOLITAN UNIV,DEPT CHEM,HACHIOJI,TOKYO 19203,JAPAN
关键词
D O I
10.1104/pp.102.4.1319
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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-degrees-C, and the activity at 30-degrees-C was one-third to one-half of that at 60-degrees-C. The system did not discriminate the L- and D-enantiomers of tryptophan.
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页码:1319 / 1324
页数:6
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