Bivalve Tropomyosins Exhibit Strong Inhibition of Actomyosin Mg-ATPase and High Viscosity
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- Nishimura Yasushi
- Department of Chemistry, Faculty of Fisheries, Hokkaido University Ajinomoto Co., Inc.
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- Ojima Takao
- Department of Chemistry, Faculty of Fisheries, Hokkaido University
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- Nishita Kiyoyoshi
- Department of Chemistry, Faculty of Fisheries, Hokkaido University
書誌事項
- タイトル別名
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- Bivalve Tropomyosins Exhibit Strong Inh
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Tropomyosins were isolated from striated and smooth adductor muscles of akazara scallop Chlamys nipponensis akazara and ezo-giant scallop Patinopecten yessoensis and smooth adductor muscle of surf clam Spisula sacharinensis. These bivalve tropomyosins inhibited Mg-ATPase activity of rabbit reconstituted actomyosin to 15% of original activity, i.e., approximately 1.4 times stronger than rabbit and carp tropomyosins did at a weight ratio of 2:1 for F-actin:tropomyosin. On the other hand, the relative viscosities in the absence of KCl were 3.5-6 times higher than those ofrabbit and carp tropomyosins. The intrinsic viscosities were, however, comparable to that of rabbit tropomyosin, i.e., 0.5 dl/g for bivalve tropomyosins and 0.4 dl/g for rabbit tropomyosin. These viscosities suggest that the bivalve tropomyosins tend to form a highly polymerized form compared with rabbit tropomyosin. Circular dichroism spectra and amino acid compositions of the bivalve tropomyosins are similar to one another and also to rabbit and carp tropomyosins. C-terminal three amino acids of bivalve tropomyosins were sequenced as-Ala-Gly-Tyr (scallops) and-Gly-Tyr-Thr (surf clam), whichare quite different from-Thr-Ser-Ile and Thr-Ser-Leu of rabbit α- and β-tropomyosin, respectively.
収録刊行物
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- Fisheries science
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Fisheries science 63 (5), 802-806, 1997
公益社団法人 日本水産学会
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詳細情報 詳細情報について
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- CRID
- 1390001204430292608
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- NII論文ID
- 130003903110
- 10004871724
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- NII書誌ID
- AA10993718
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- COI
- 1:CAS:528:DyaK2sXntVGrur0%3D
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- NDL書誌ID
- 4326637
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- ISSN
- 09199268
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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- 使用不可