Stability of Fish Myosins and Their Fragments to High Hydrostatic Pressure
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- Ishizaki Shoichiro
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Tanaka Munehiko
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Takai Rikuo
- Department of Food Science and Technology, Tokyo University of Fisheries
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- Taguchi Takeshi
- Department of Food Science and Technology, Tokyo University of Fisheries
Bibliographic Information
- Other Title
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- Stability of Fish Myosins and Their Fra
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Abstract
The stability of black marlin and jack mackerel myosins and their fragments to high hydrostatic pressure (100, 200, 300, 400, and 500 MPa) was examined by meansof a solubility test, CD measurement, and changes in fluorescence intensity. The solubility of both myosins decreased with the hydrostatic pressure-treatment above 300 MPa. There was a marked decrease in thesolubility of S-1, especially in the presence of 0.05M KCl, though the solubility of rod did not alter. The results of CD measurements showed a slight decrease in the helical content of myosins and S-1s. From the data of binding of ANS (8-anilino-1-naphthalene sulfonate), it was indicated that by pressure treatment the fluorescence intensities of myosins and S-ls increased rapidly. By the changes of tryptophan fluorescence intensity the pressure-treated S-1s in 0.05M KCl showed rapidly decreasing curves. The pressure-stability of S-1s in 0.05M KCl was very inferior to that of S-1s in 0.6M KCl.
Journal
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- Fisheries science
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Fisheries science 61 (6), 989-992, 1995
The Japanese Society of Fisheries Science
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Details 詳細情報について
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- CRID
- 1390001204428877184
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- NII Article ID
- 130003902830
- 10004864309
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- NII Book ID
- AA10993718
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- NDL BIB ID
- 3920574
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- ISSN
- 09199268
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed