1999 Fiscal Year Final Research Report Summary
Molecular properties of cytochrome c oxidase in Ascaris respiratory chain and its response to oxygen tension
| Project/Area Number |
10670239
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
寄生虫学(含医用動物学)
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| Research Institution | Juntendo University |
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Principal Investigator |
TAKAMIYA Shinzaburo Juntendo University, Dept.of Parasitol., Associate Professor, 医学部, 助教授 (90138206)
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| Co-Investigator(Kenkyū-buntansha) |
YAMASAKI Hiroshi Juntendo University, Dept.of Parasitol., Lecturer, 医学部, 講師 (00138207)
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| Project Period (FY) |
1998 – 1999
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| Keywords | Ascaris suum / respiratory chain / cytochrome c oxidase / response to oxygen tension / C. elegans / Rhodoquinone / fumarate reductase / complex II |
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| Research Abstract |
1.Achievement in l998: The respiratory chain of Caenorhabditis elegans was characterized in mitochondria isolated from aerobically grown nematodes. Nematode mitochondria contain ubiquinone-9 as a major component and rhodoquinone-9 as a minor component. The ratio of ubiquinone-9/rhodoquinone-9 is higher in C. elegans mitochondria than in mitochondria from second-stage larvae of Ascaris suum, the free-living stage of porcine gut-dwelling nematode. The individual oxidoreductase activities comprising succinate-oxidase and the amount of substrate-reducible cytochromes are comparable to those of mitochondria from second-stage larvae of A. suum. The specific activity of fumarate reductase is lower in C. elegans mitochondria than in mitochondria from second-stage larvae of A. suum, but still higher than in mammalian mitochondria. These results indicate that the free-living nematode C. elegans is capable of synthesizing rhodoquinone, as distinguished from aerobic mammalian species, although its mitochondria appear more aerobic than A. suum larval mitochondria.
2. Achievement in 1999: The Ip subunit of Ascaris suum larval complex II was characterized because Northern hybridization showed that the adult Ip also is expressed in the larvae. The Ip of larval complex II was recognized by the antibody against adult Ip, and was indistinguishable from the adult Ip by peptide mapping. The N-terminal 42 amino acid sequence of Ip in the larval complex II purified by DEAE-cellulofine column chromatography was identical to that of the mature form of the adult Ip. Furthermore, the amino acid composition of larval Ip determined by micro-analysis on a PVDF membrane is almost the same as that of adult Ip. These results suggest that the two different stage-specific forms of the A. suum complex II share a common Ip subunit, even though the adult enzyme functions as a fumarate reductase, while larval enzyme acts as a succinate dehydrogenase.
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Research Products
(4 results)
