alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus
- Contributor(s):
- Anfinsen, Christian B. (Christian Boehmer), 1916-1995 Uemori, T. Laderman, Kenneth A. Kato, I. Taguchi, Y. Journal of Biological Chemistry Asada, Kiyozo Mukai, H.
- Publication:
- American Society for Biochemistry and Molecular Biology, 15 November 1993
- Language(s):
- English
- Format:
- Text
- Subject(s):
- alpha-Amylases Pyrococcus furiosus Recombinant Proteins Amino Acid Sequence
- Genre(s):
- Archival Materials Articles
- Abstract:
- In this article, Anfinsen, et al, reported that while trying to study the factors that influenced protein thermostability, or the ability to remain stable at relatively high temperatures, they had cloned a gene from the hyperthermophilic bacterium Pyrococcus furiosus encoded with a highly thermostable alpha-amylase and expressed it in Escherichia Coli. The alpha-amylase expressed in E. Coli exhibited the temperature-dependent activation characteristic of the original enzyme from P. furiosus, but had a higher apparent molecular weight that was attributed to the improper formation of the native quaternary structure.
- Copyright:
- This item may be under copyright protection; contact the copyright owner for permission before re-use.
- Extent:
- 6 pages
- NLM Unique ID:
- 101584571X158 (See in Profiles in Science)
- Profiles in Science ID:
- KKBBKP
- Permanent Link:
- http://resource.nlm.nih.gov/101584571X158
- Archival Collection:
- The Christian B. Anfinsen Papers (Profiles in Science)