alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus alpha-Amylases Pyrococcus furiosus Recombinant Proteins Amino Acid Sequence 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. American Society for Biochemistry and Molecular Biology, 15 November 1993 The American Society for Biochemistry and Molecular Biology, 15 November 1993 Journal of Biological Chemistry Laderman, Kenneth A. Asada, Kiyozo Uemori, T. Mukai, H. Taguchi, Y. Kato, I. Anfinsen, Christian B. Anfinsen, Christian B. Articles Archival Materials Text 6 pages nlm:nlmuid-101584571X158-doc 101584571X158 http://resource.nlm.nih.gov/101584571X158 Profiles ID: KKBBKP English Profiles in Science