The Purification and Characterization of an Extremely Thermostable alpha-Amylase from the Hyperthermophilic Archaebacterium
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)
1993-11-15 (November 15, 1993)
Laderman, Kenneth A.
Davis, Bradley R.
Krutzsch, Henry C.
Lewis, Marc S.
Griko, Y. V.
Privalov, Peter L.
Anfinsen, Christian B.
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.
American Society for Biochemistry and Molecular Biology
Reproduced with permission of the American Society for Biochemistry and Molecular Biology.