Comparison of the Thermal Stabilities of the .ALPHA..BETA. Heterodimer and the .ALPHA. Subunit of Avian Myeloblastosis Virus Reverse Transcriptase

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  • KONISHI Atsushi
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • NEMOTO Daisuke
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • YASUKAWA Kiyoshi
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University
  • INOUYE Kuniyo
    Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University

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  • Comparison of the thermal stabilities of the αβ heterodimer and the α subunit of avian myeloblastosis virus reverse transcriptase
  • Comparison of the thermal stabilities of the av heterodimer and the a subunit of avian myeloblastosis virus reverse transcriptase

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Abstract

Avian myeloblastosis virus reverse transcriptase (AMV RT) is a heterodimer consisting of a 63-kDa α subunit and a 95-kDa β subunit. In this study, we explored the role of the interaction between the α and β subunits on AMV RT stability. The recombinant AMV RT α subunit was expressed in insect cells and purified. It exhibited lower thermal stability than the native AMV RT αβ heterodimer. Unlike the αβ heterodimer, the α subunit was not stabilized by template-primer. These results suggest that interaction between the α and β subunits is important for AMV RT stability.

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