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Studies on Myofibrils from the Stored Muscle
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- YANG Ryung
- Department of Agricultural Chemistry, University of Tokyo
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- OKITANI Akihiro
- Department of Agricultural Chemistry, University of Tokyo
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- FUJIMAKI Masao
- Department of Agricultural Chemistry, University of Tokyo
Bibliographic Information
- Other Title
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- Part I. Post-mortem Changes in Adenosine Triphosphatase Activity of Myofibrils from Rabbit Muscle
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Description
Adenosine triphosphatase (ATPase) activity of myofibrils isolated from fresh muscle and the muscle stored at 4°C have been measured.<br> An increase in Mg-activated ATPase activity of myofibrils was caused by lengthened homogenization.<br> With the progress of aging of muscle, Mg-activated ATPase activity of myofibrils increased remarkably.<br> When myofibrils from pre-rigor and rigor muscle in 0.16M KCl were treated with 0.6M KCl18mM Tris-maleate solution (pH 7.0), Mg-activated ATPase activity of myofibrils at low ionic strength increased markedly. However, the Mg-activated ATPase activity of the myofibril isolated from the muscle stored at 4°C for 8 days (8-myofibril) increased slightly after the similar treatment.<br> The dependence of myofibrillar ATPase activity on KCl concentration became greater with the progress of aging of muscle.<br> These results may show that, as long as ATPase activity and the dependence of ATPase activity on KCl concentration are concerned, 8-myofibril is the most similar to the isolated actomyosin among myofibrils, although actomyosin in muscle may exist in a different form from that in solution. It is suggested that, with the progress of aging, the structural alteration of myofibril occurred and the myofibril became more susceptible to ATP-induced transformation.
Journal
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 34 (12), 1765-1772, 1970
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681444662144
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- NII Article ID
- 130003523288
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- COI
- 1:CAS:528:DyaE3MXktFOjtLk%3D
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- ISSN
- 18811280
- 00021369
- http://id.crossref.org/issn/00021369
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
- OpenAIRE
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- Abstract License Flag
- Disallowed
