Official websites use .gov A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS A lock ( ) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
Anfinsen believed that the discovery of hyperthermophilic bacteria in the early 1980s provided a valuable tool for the analysis of protein stability, because these bacteria made it possible to study the molecular mechanisms that governed structure and function in a system adapted for elevated temperatures. In this article, Anfinsen, et al, reported that they had purified to homogeneity the alpha-amylase, an enzyme that degrades starch, from the hyperthermophilic archaebacterium Pyrococcus furiosus. Due to the large amount of data available on alpha-amylase, Anfinsen believed that the enzyme was a "favorable" choice for the comparison of mesophilic, or optimal temperature-loving, and Thermophilic enzymes.
Amino Acid Sequence, Enzyme Stability, and Pyrococcus furiosus
Format:
Text
Extent:
8 pages
Language:
English
Legacy Source Citation:
Periodical. Laderman, Kenneth A., Bradley R. Davis, Henry C. Krutzsch, Marc S. Lewis, Y. V. Griko, Peter L. Privalov, and Christian B. Anfinsen. "The Purification and Characterization of an Extremely Thermostable alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus." Journal of Biological Chemistry 268, 32 (15 November 1993): 24394-24401. Article. 8 Images.. Journal of Biological Chemistry