| Project/Area Number |
10670048
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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 physiology
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| Research Institution | Teikyo University |
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Principal Investigator |
SUGI Haruo Teikyou Univ. Sch of Med., Professor, 医学部, 教授 (20082076)
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| Co-Investigator(Kenkyū-buntansha) |
SHIRAKAWA Ibuki Teikyou Univ. Sch.of Med. Instructor, 医学部, 助手 (80236190)
CHAEN Sigeru Teikyou Univ. Sch.of Med. Assistant Professor, 医学部, 講師 (60142452)
KOBAYASHI Takakazu Teikyou Univ. Sch.of Med. Assistant Professor, 医学部, 講師 (00112756)
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| Project Period (FY) |
1998 – 1999
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| Project Status |
Completed (Fiscal Year 1999)
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| Budget Amount *help |
¥3,200,000 (Direct Cost: ¥3,200,000)
Fiscal Year 1999: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1998: ¥2,700,000 (Direct Cost: ¥2,700,000)
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| Keywords | muscle contraction / ATPase activity / contraction characteristics / muscle fatigue / muscle metabolites |
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| Research Abstract |
The results of the above research project are summarized as follows:
1. The effect of L(+)-lactate on the contraction characteristics and ATPase activity of single glycerol-extracted muscle fibers prepared from rabbit psoas muscle was studied by simultaneously recording CaィイD12+ィエD1-activated isometric tension, muscle fiber stiffness and ATPase activity in the presence and absence of lactate.
2. The maximum isometric force and stiffness decreased roughly in paralleled by 2-10% with increasing lactate concentration from 5 to 25 mM.
3. The pCa-tension and pCa-ATPase activity relations did not change appreciably in the presence of lactate.
4. The tension cost, obtained from the ATPase activity during steady isometric force generation, decreased by about 8% in the presence of 25 mM lactate.
5. The unloaded in vitro sliding between fluorescently labeled actin filaments and myosin decreased by about 10% in the presence of 25 mM lactate,
6. These results indicate that lactate reduces the efficiency, with which chemical energy derived from ATP hydrolysis ins converted into mechanical work.
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