Biochemical studies on marine animal muscle proteins
| Project/Area Number |
62304023
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| Research Category |
Grant-in-Aid for Co-operative Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Fisheries chemistry
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| Research Institution | University of Tokyo |
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Principal Investigator |
HASHIMOTO Kanehisa Professor, Faculty of Agriculture, University of Tokyo, 農学部, 教授 (30011828)
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| Co-Investigator(Kenkyū-buntansha) |
NISHIMOTO Jun-ichi Professor, Faculty of Fisheries, Kagashima University, 水産学部, 教授 (30041693)
SHIMIZU Yutaka Professor, Faculty of Agriculture, Kyoto University, 農学部, 教授 (50036696)
KIMURA Shigeru Assistant Professor, Faculty of Fisheries, Tokyo University of Fisheries, 水産学部, 助教授 (10017056)
ARAI Ken-ichi Professor, Faculty of Fisheries, Hokkaido University, 水産学部, 教授 (20001597)
WATABE Shugo Instructor, Faculty of Agriculture, University of Tokyo, 農学部, 助手 (40111489)
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| Project Period (FY) |
1987 – 1988
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| Project Status |
Completed (Fiscal Year 1988)
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| Budget Amount *help |
¥25,000,000 (Direct Cost: ¥25,000,000)
Fiscal Year 1988: ¥11,000,000 (Direct Cost: ¥11,000,000)
Fiscal Year 1987: ¥14,000,000 (Direct Cost: ¥14,000,000)
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| Keywords | Myosin / Actin / Tropomyosin / Collagen / Troponin / Calpain / Paramyosin / Aldolase / Fish muscle / Gel-forming ability / サメ / ミオシン軽領 / ミオシン・サブフラグメント1 / グリセルアルデヒド-3-リン酸脱水素酵素 / ミオシン軽鎖 / フィラメント形成能 / アクチン / グリセルアルデヒドー3ーリン酸脱水素酵素 / 筋原線維 / 大正エビ |
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| Research Abstract |
One of major protein resources for human consumption is marine animal mucsles in Japan therefore, biochenical studies on muscle proteins from them have been one of the most inportant fields in fisheries science there and provided useful information for disheries processing and food engineering. A marked recent propress developed in protein chemistry and enqineering stimulated us to have the present research project to disclose the properties of marine animal muscle proteins in the viewpoint of comparative biochemistry, thus making it possible to utilize these proteins more effectively.
1. Myosin subfragment l(S1) with alkali l(A1) light chain of fish ordinary muscle was successfully separated from S1(S2) and found to have lower atpase activity and thermostability than those of S1(A2). Correspondingly, A1 light chain exibited different physicochemical and immunological properties from those of A2. Fish myosin was demonstrated to be endowed with a poor filament-forming ability which was i
… More
mproved in the presence of MgC12 over 5mM.
2. Fleshy prawn muscle and subcuticular collagen was demonstrated to be composed of ( 1)_3 homotrimer. Akazara scallop troponin consisted of 52k, 40k and 20k components, while paramyosin from bivalve adductor muscle was phosphorylated at a high rate. These results suggest that invertabrate muscle proteins have many different properties from those of vertebrate.
3. Fish calpain exerted its proteopytic activity only on a denatured myosin, thus demonstrating its characteristic feature to recognize the substrate structure.
4. Fish aldolase was bound to actomyosin, although its effect on the gel-forming ability of fish muscle remained unclear. Myosin and paramyosin were shown to play a primary role in fish muscle gelation, while tropomyosin was not. Myosin from elasmobranch was resistant against urea denaturation compared with teleost myosin and produced a strong gel strength when mixed with salt and heated. Setting phenomenon was hardly observed with elasmobranch myosin sol in the presence of salt. Less
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Report
(3 results)
Research Products
(19 results)
