Purification of an Auxin-Binding Protein from Etiolated Mung Bean Seedlings by Affinity Chromatography

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概要

• 論文の詳細を見る

• An auxin-binding protein with high affinity for 2,4-D and IAA was purified from the extract of etiolated mung bean seedlings by affinity chromatography on 2,4-D-linked Sepharose 4B and by gel filtration on Sepharose 4B. Its molecular weight was estimated to be about 390,000 by gel filtration on Sepharose 4B and it consisted of two different subunits with molecular weights of about 47,000 and 15,000. This protein had no ribulose-1,5-bisphosphate carboxylase activity. Its dissociation constants for 2,4-D and IAA were 9.3 × 10^<-6> M and 3.2 × 10^<-6> M, respectively, as determined by Scatchard's method.

• 日本植物生理学会の論文

著者

• Sakai Shingo

  Laboratory Of Cell Biochemistry Faculty Of Science Saitama University

• Sakai Shingo

  Laboralory Of Cell Biochemistry Faculty Of Science Saitama University

• Hanagata Toshio

  Laboratory of Cell Biochemistry, Faculty of Science, Saitama University

• Hanagata Toshio

  Laboratory Of Cell Biochemistry Faculty Of Science Saitama University

関連論文

• Modulation of Gene Expression in Isolated Nuclei by Auxin-Binding Proteins
• Stimulation of RNA Synthesis in Isolated Nuclei by Auxin-Binding Proteins-I and -II
• Auxin-Binding Protein in Etiolated Mung Bean Seedlings : Purification and Properties of Auxin-Binding Protein-II
• Purification of an Auxin-Binding Protein from Etiolated Mung Bean Seedlings by Affinity Chromatography
• Biosynthesis of ethylene in sweet potato root tissue
• Effects of the Inhibitory Protein of Ethylene Synthesis on ATP Levels in Mung Bean Hypocotyl Segments
• Characterization of 2, 4-D Binding to the Auxin-binding Protein Purified from Etiolated MungBean Seedlings

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