| Project/Area Number |
01540557
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
植物生理学
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| Research Institution | Hokkaido University |
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Principal Investigator |
OKUYAMA Hidetoshi Hokkaido Univ. Fac. Science ; Associate Professor., 理学部, 助教授 (90125295)
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| Co-Investigator(Kenkyū-buntansha) |
TAKADA Yasuhiro Hokkaido Univ., Fac. Science Lecturer., 理学部, 講師 (10163213)
佐々木 昭治 北海道大学, 理学部, 教授 (10000811)
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| Project Period (FY) |
1989 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1991: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1990: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1989: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | Psychrotroph / Pseudomonas / Psychrophile / Vibrio / cis / trans isomerase / trans-Unsaturated fatty acid / Pseudomonas / シス・トランス異性化酵素 / 脂肪酸 / 低温適応 / Vibrio ABE-1株 / 不飽和脂肪酸異性化酵素 |
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| Research Abstract |
Cell-free extract of PseudoNonas sp. strain E-3 catalyzed the conversion of 9cis-hexadecenoib acid[16 : 1(9c)]in a free acid and 16 : 1(9c)esterified to both the sn-1 and 2 positions of phosphatidylethanolamine(PE)to 9-trans-hexadecenoic acid[16 : 1(9t)]. The cell-free extract wa!j separated into the soluble(cytosolic)and membrane fractions by the ultracentrifugation at 105, 000 x g for 60 min. The cytosol fraction catalyzed the isomerization of the free 16 : 1(9c). On the other hand, it isomerized 16 : 1(9c)esterified to PE in the presence of the membrane fraction. One cytosolic component(component I)that catalyze the isomerization of free 16 : 1(9c)and the other(component II)that is needed for the isomerization of esterified 16 : 1(9c)were completely separable one another with a high-performance liquid chromatographic system equipped Kith a gel filtration column. These results suggest that Psedomonas sp. strain E-3 contains at least two types of "Cis/trans isometases.
Component I was purified by column chromatography with DEAE-Toyopearl and ButyToyopearl. Purified enzyme was separated into two components by gel-filtration column chromatography. These two components ' were essentially needed for isomeriation of 16 : 1(9c)to 16 : 1(9t). The enzyme has a temperature optimum at ^oC and maintained significant activities at subzero temperatures.
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