2003 Fiscal Year Final Research Report Summary
Environmental acclimation of molluscan are related to a new mechanism for economizing energy
| Project/Area Number |
13660196
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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 |
General fisheries
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| Research Institution | Ishikawa Agricultural College |
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Principal Investigator |
ENOMOTO Toshiki Ishikawa Agricultural College, Food Science, Professor, 食品科学科, 助教授 (70203643)
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| Co-Investigator(Kenkyū-buntansha) |
KUDA Takashi Ishikawa Agricultural College, Food Science, Associate Professor, 食品科学科, 助教授 (00290081)
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| Project Period (FY) |
2001 – 2003
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| Keywords | Mollusca / Osmotic regulation / Anaerobiosis / Phosphofructokinase / Adenylates / Energy metabolism / Environmental acclimation / Opine fermentation |
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| Research Abstract |
Some glycolytic metabolites in the adductor muscle were measured after transfer of scallops from aerobic to anaerobic saltwater for 12 h. The level of octopine increased gradually during the initial 3h incubation, and thereafter the level increased rapidly up to 12 h. The ATP level also did not show any significant change for the initial 3 h, and then decreased rapidly. In the short-term effects of anaerobiosis for 90 min, the level of Fru 6-P increased just after transfer to anaerobiosis, and then its level decreased. In contrast, Fru 1,6-BP level increased gradually, at the time when both Glc 6-P and Fru 6-P decreased. The AMP was accumulated drastically in contrast with the decrease of ATP. When the same experiments were done by using clams, change in the AMP level reflected those of ATP, and the AMP level in anaerobic clams was about twice as high as in aerobic one at the end of acclimation. These results strongly suggest that molluscan PFK exhibits a low degree of specificity for phosphate donors. Thus, PFK was purified to homogeneity from adductor muscle of scallops, and specificity for phosphate donors was studied. Scallop PFK exhibits a low degree of specificity for phosphate donors, especially ADP. Based on partial amino acid sequences of the purified PFK, it was tried that cDNA of the enzyme is cloned. Complete primary structure of the PFK determined by cDNA cloning remains to be examined.
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