The Purification and Characterization of an Extremely Thermostable alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus
Dates
- Publication: 15 November 1993
Extent
8 pages
Creator
- Anfinsen, Christian B. (Christian Boehmer), 1916-1995 (Creator, Person)
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
Physical Description
Physical Condition - Good
Creator
- Anfinsen, Christian B. (Christian Boehmer), 1916-1995 (Creator, Person)
Collecting Area Details
Part of the Archives and Modern Manuscripts Collections Collecting Area
8600 Rockville Pike
Bldg 38/1E-21, MSC 3819
Bethesda MD 20894 US
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