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- YABE Kazuo
- Chemical Laboratory, Kushiro College, Hokkaido University of Education
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- NAKAMURA Kazuharu
- Kashiwa Primary School
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- SUZUKI Mieko
- Chemical Laboratory, Kushiro College, Hokkaido University of Education
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- ITO Yasuzo
- Chemical Laboratory, Kushiro College, Hokkaido University of Education
Bibliographic Information
- Other Title
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- 寒帯産魚類アクトミオシンの温度安定性など生化学的性質
- 寒帯産魚類アクトミオシンの温度安定性など生化学的性質について
- カンタイサン ギョルイ アクトミオシン ノ オンド アンテイセイ ナド セイカ
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Description
Actomyosins were prepared from the dorsal muscles of various fish species living in the frigid water zone and their biochemical activities were investigated.<br> 1) The specific Ca2+-ATpase activity of these actomyosins was generally lower than that of fishes living in the temperate water zone.<br> 2) The frigid water fish actomyosins exhibited a slightly lower ATP sensitivity than that of the temperater water fish actomyosin. Thermal inactivation of the Ca2+-ATPase activity of the former actomyosins was exactly of the first order reaction. These results suggest the presence of some actomyosin aggregates in the present actomyosin preparations.<br> 3) It was found by comparison of the inactivation rate constants of Ca2+-ATPase at 30°C that the actomyosins from Salmonidae and Osmeridae are 3-8 and 6-9 times, respectively, more unstable than that of carp. The actomyosins from some deep sea fishes of the North Pacific Ocean were more than 18 times less stable compared to that of carp.<br> 4) No clear relationship was found to exist between the inactivation rate constants of the actomvosins and their biochemical activities, such as specific Ca2+-ATPase activity and ATP-sensitivity.
Journal
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- NIPPON SUISAN GAKKAISHI
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NIPPON SUISAN GAKKAISHI 44 (12), 1345-1350, 1978
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
- 1390282681390559744
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- NII Article ID
- 130001547985
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- NII Book ID
- AN00193422
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- ISSN
- 1349998X
- 00215392
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- NDL BIB ID
- 2036035
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- Text Lang
- ja
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- Article Type
- journal article
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- Data Source
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- JaLC
- IRDB
- NDL Search
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed