2006 Fiscal Year Final Research Report Summary
Elucidation of the substrate specificity mechanism of phospholipase A2 from marine organisms
| Project/Area Number |
15580175
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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 |
Fisheries chemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
KISHIMURA Hideki Hokkaido University, Faculty of Fisheries Sciences, Associate Professor, 大学院水産科学研究院, 助教授 (50204855)
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| Co-Investigator(Kenkyū-buntansha) |
OJIMA Takao Hokkaido University, Faculty of Fisheries Sciences, Professor, 大学院水産科学研究院, 教授 (30160865)
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| Project Period (FY) |
2003 – 2006
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| Keywords | Marine invertebrate / Echinoderm / Asterina pectinifera / Phospholipase A2 / Mutant / Substrate specificity / Specific activity / Pancreatic loop |
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| Research Abstract |
1.The specific activities of the mutants that were introduced Lys residue in pancreatic loop region for phosphatidylcholine were lower than that of native phospholipase A2 (PLA2) from the pyloric ceca of the starfish.4sterinapectinira, similarly to that of porcine pancreatic PLA2. It was suggested that the charge and structure of pancreatic loop region of the starfish PLA2 might carry out important role on polar-group specificity.
2.The PLA2 isozyme from the starfish A. pectinifera and the PLA2s from other starfish species well hydrolyzed phosphatidylcholine similar to the PLA2 from the starfish A. pectinifera It was suggested that the polar-group specificity of the starfish PLA2 might common property with the PLA2 from Asteroid.
3.The PLA2 activity of the starfish A. pectinifera was very high in every seasons and areas, whereas, the PLA2 activity of the starfish juvenile was extremely lower than that of the mature starfish. It was suggested that the very high activity
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Research Products
(12 results)
