| Project/Area Number |
02454046
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
園芸・造園学
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| Research Institution | Nagoya University |
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Principal Investigator |
YAMAKI Shohei Nagoya University, Professor School of Agriculture, 農学部, 教授 (70210341)
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| Co-Investigator(Kenkyū-buntansha) |
OHNO Hajime Nagoya University, Agriculture Assistant Professor, 農学部, 助手 (20126840)
TEZUKA Takafumi Nagoya University, Agriculture Associate Professor, 農学部, 助教授 (10109316)
SAKAI Shingo Tukuba University, Biological Science Associate Professor, 生物科学系, 助教授 (60033388)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥7,600,000 (Direct Cost: ¥7,600,000)
Fiscal Year 1991: ¥2,400,000 (Direct Cost: ¥2,400,000)
Fiscal Year 1990: ¥5,200,000 (Direct Cost: ¥5,200,000)
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| Keywords | Auxin / IAA / Auxin-binding protein / Protoplast / Melon / Apple / Cymbidium / プロトプラスト |
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| Research Abstract |
Auxin-binding protein in apple seedling was partially purified by 2, 4-D linked-Sephasrose 4B affinity chromatography and 2 times of Sepharose 4B gel filtration. It had a molecular weight of about 400 KDa and was composed of subunit bands of 56 KDa ana 15 KDa by SDS-PAGE, which appeared in proportion to the strength of 6binding activity. The dissociation constant by Scatchard plot was 7.7X1O^<-6> M. This binding protT4n is similar to ABP-I from mung bean seedling. The binding activity to ^<14>C-IAA was completely inhibited by 2, 4-D and NAA, and inhibited to about 50% by PCIB of antiauxin. Auxin-binding protein in melon seedling partially purified by the same procedure showed the equal activity between both assay methods of an ammonium sulfate precipitation and an equilibrating dialysis. The protein had a molecular weight of 155 KDa and a dissociation constant of 4.8X1O^<-6> M, and combined more than one molar IAA to one molar protein. This binding protein from mellon seedling is like ABP-II from mung bean seedling.
The function about two kinds of the auxin-binding protein was not investigated in detail through the present experiment. However, we can suggest firmly these auxin binding proteins possess the characteristics as an auxin receptor, as defined by the specificity for substrate, the saturation of reaction to substrate concentration and the reversibility of reaction.
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