The increase of fragility of sarcoplasmic reticulum in frozen fish muscle.
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- HANAOKA Kem'ichi
- Lab. Fish. Tech., Fac. Agr., Kyushu Univ.
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- TOYOMIZU Masamichi
- Lab. Fish. Tech., Fac. Agr., Kyushu Univ.
Bibliographic Information
- Other Title
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- 凍結貯蔵魚肉における筋小胞体の脆弱化
- 凍結貯蔵魚肉における筋小胞体の脆弱化〔英文〕
- トウケツ チョゾウ ギョニク ニ オケル キン ショウホウタイ ノ ゼイジャッ
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Abstract
Phospholipids (PL) are enzymatically decomposed even in frozen fish muscle; the most rapid decomposition rate occurs at -5°C. In order to clarify the fragility of a biological membrane, sarcoplasmic reticulum (SR), due to PL decomposition, the authors prepared microsomes at intervals from carp ordinary muscle stored at -5°C and studied their alterations in terms of yield and appearance. The yield of microsomes was estimated from the protein amount determined by a biuret method; their appearance was observed by freeze-etching electron microscopy.<br> The yield linearly decreased with storage; it was one-half of the original value when 50% of the PL seemed to be decomposed. The appearance of microsomes prepared from muscle stored for 11 days was not markedly different from that immediately after death, but details of some concave fracture faces showed an irregular distribution of particles. The appearance of that for 22 days showed particle clusters in some parts and some disturbed outlines of faces. The appearance of that for 50 days showed few normal faces; the diameters of faces had decreased and many indefinitely shaped particle clusters had formed.<br> These results confirm that PL decomposition results in the fragility of SR membrane, even though this is not clearly recognized by observations of the appearance of SR itself.
Journal
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- NIPPON SUISAN GAKKAISHI
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NIPPON SUISAN GAKKAISHI 47 (6), 765-768, 1981
The Japanese Society of Fisheries Science
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Keywords
Details 詳細情報について
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- CRID
- 1390001206412211328
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- NII Article ID
- 130001547217
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- NII Book ID
- AN00193422
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- ISSN
- 1349998X
- 00215392
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- NDL BIB ID
- 2318328
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- Text Lang
- en
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- Data Source
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- JaLC
- IRDB
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed