2011 Fiscal Year Final Research Report
Expression, purification and function of recombinant connectin domains involved in meat tenderization during postmortem aging.
| Project/Area Number |
21580330
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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 |
Zootechnical science/Grassland science
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| Research Institution | Kobe University |
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Principal Investigator |
YAMANOUE Minoru 神戸大学, 大学院・農学研究科, 准教授 (30182596)
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| Co-Investigator(Renkei-kenkyūsha) |
UEDA Syuji 神戸大学, 大学院・農学研究科, 助教 (50379400)
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| Project Period (FY) |
2009 – 2011
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| Keywords | 食肉 / 熟成 / コネクチン / パラトロポミオシン / 遺伝子クローニング / 遺伝子発現 |
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| Research Abstract |
A myofibrillar protein, paratropomyosin weakens the rigor linkages between actin and myosin, and contributes to meat tenderization. Paratropomyosin was found at the A-I junction of myofibrils in living muscle and in muscle immediately postmortem. In chicken breast muscle paratropomyosin binds to connectin when examining binding of paratropomyosin at the A-I junction. In the present study, we produced all recombinant domains that constituted the connectin fragment at the junction and examined binding of paratropomyosin to each domain on PVDF membrane in order to clarify more precise binding site in connectin molecule. On the other hand, polyclonal and monoclonal antibodies produced against the connectin 20-kDa fragment, which was located in The Z-disk region and increased in chicken sarcoplasm with postmortem aging, were characterized in order to utilize for estimating meat aging.
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Research Products
(13 results)
