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alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus

 Digital Record
Identifier: 101584571X158


  • Publication: 15 November 1993


6 Pages



In this article, Anfinsen, et al, reported that while trying to study the factors that influenced protein thermostability, or the ability to remain stable at relatively high temperatures, they had cloned a gene from the hyperthermophilic bacterium Pyrococcus furiosus encoded with a highly thermostable alpha-amylase and expressed it in Escherichia Coli. The alpha-amylase expressed in E. Coli exhibited the temperature-dependent activation characteristic of the original enzyme from P. furiosus, but had a higher apparent molecular weight that was attributed to the improper formation of the native quaternary structure.

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Laderman, Kenneth A., Kiyozo Asada, T. Uemori, H. Mukai, Y. Taguchi, I. Kato, and Christian B. Anfinsen. "alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus." Journal of Biological Chemistry 268, 32 (15 November 1993): 24402-24407. Article. 6 Images.

Journal of Biological Chemistry

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Physical Condition - Good

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Part of the Archives and Modern Manuscripts Collection Collecting Area

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