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The Purification and Characterization of an Extremely Thermostable alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus

 Digital Record
Identifier: 101584571X157

Dates

  • Publication: 15 November 1993

Extent

8 pages

Creator

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.

Language of Materials

English

Original Profiles System Identifier

KKBBKN

Source Category

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

Physical Description

Physical Condition - Good

Collecting Area Details

Part of the Archives and Modern Manuscripts Collections Collecting Area

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