Authors:
Andrea Vig University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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Réka Dudás University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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Tünde Kupi University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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J. Orbán University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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G. Hild University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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D. Lőrinczy University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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M. Nyitrai University of Pécs Faculty of Medicine, Department of Biophysics Szigeti str. 12 Pécs 7624 Hungary

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Abstract  

The effect of phalloidin on filaments polymerized from ADP-actin monomers of the heart muscle was investigated with differential scanning calorimetry. Heart muscle contains α-skeletal and α-cardiac actin isoforms. In the absence of phalloidin the melting temperature was 55°C for the α-cardiac actin isoform and 58°C for the α-skeletal one when the filaments were generated from ADP-actin monomers. After the binding of phalloidin the melting temperature was isoform independent (85.5°C). We concluded that phalloidin stabilized the actin filaments of α-skeletal and α-cardiac actin isoforms to the same extent when they were polymerized from ADP-actin monomers.

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation
1969
Volumes
per Year
1
Issues
per Year
24
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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