The Purification and Characterization of an Extremely Thermostable alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus
Description:
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.
Number of Image Pages:
8 (1,479,701 Bytes)
Date:
1993-11-15 (November 15, 1993)
Creator:
Laderman, Kenneth A.
Davis, Bradley R.
Krutzsch, Henry C.
Lewis, Marc S.
Griko, Y. V.
Privalov, Peter L.
Anfinsen, Christian B.
Source:
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.
Publisher:
American Society for Biochemistry and Molecular Biology
Rights:
Reproduced with permission of the American Society for Biochemistry and Molecular Biology.
