Thermal Unfolding of the Cold-acclimated Type of Carp Light Meromyosin Expressed by Recombinant DNA in <i>Escherichia coli</i>
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- Kakinuma Makoto
- Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
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- Funabara Daisuke
- Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
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- Nakaya Misako
- Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
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- Hirayama Yasushi
- Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
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- Watabe Shugo
- Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo
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- Maeda Kayo
- International Institute for Advanced Research, Matsushita Electric Industrial Co., Ltd.
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- Ooi Tatsuo
- Department of Food Science, Kyoto Women's University
Bibliographic Information
- Other Title
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- Thermal Unfolding of the Cold-acclimated Type of Carp Light Meromyosin Expressed by Recombinant DNA in Escherichia coli
- Thermal Unfolding of the Cold-acclimate
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Abstract
cDNA encoding fast skeletal muscle light meromyosin (LMM) predominantly expressed in carp acclimated to a cold temperature of 10°C was inserted into an Escherichia coli expression vector pET-11a. The resulting plasmid pET10 produced non-fused carp 10°C-type LMM, yielding 10% of the total proteins in E. coli. The 10°C-type LMM was purified by altered dialyses against high- and low-ionic-strength buffers and ion-exchange chromatography. An apparent molecular mass of the purified LMM was about 74, 000 on SDS-PAGE, which was slightly larger than that previously reported for LMM isolated from carp acclimated to 10°C. Transition temperatures (Tm) were 30.2 and 34.9°C for the present 10°C-type LMM on DSC analysis. This LMM exhibited a typical pattern of α-helix in CD spectroscopy with two minima at 222 and 208 nm, and its α-helical content at 20°C was about 70%. The maximal decreasing rate derivative at 35°C of the mean residue ellipticity of carp LMM per unit change of measuring temperature well reflected Tm values observed in DSC analysis.
Journal
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- Fisheries science
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Fisheries science 63 (6), 1008-1013, 1997
The Japanese Society of Fisheries Science
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Details 詳細情報について
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- CRID
- 1390282679405603968
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- NII Article ID
- 130003903147
- 10004872614
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- NII Book ID
- AA10993718
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- COI
- 1:CAS:528:DyaK1cXht1Sg
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- NDL BIB ID
- 4371633
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- ISSN
- 09199268
- http://id.crossref.org/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