alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus
Description:
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.
Number of Image Pages:
6 (1,010,216 Bytes)
Date:
1993-11-15 (November 15, 1993)
Creator:
Laderman, Kenneth A.
Asada, Kiyozo
Uemori, T.
Mukai, H.
Taguchi, Y.
Kato, I.
Anfinsen, Christian B.
Source:
Periodical: Laderman, Kenneth A., Kiyozo Asada, T. Uemori, H. Mukai, Y. Taguchi, I. Kato, and Christian B. Anfinsen. "alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus." Journal of Biological Chemistry 268, 32 (15 November 1993): 24402-24407. Article. 6 Images.
Publisher:
American Society for Biochemistry and Molecular Biology
Rights:
Reproduced with permission of the American Society for Biochemistry and Molecular Biology.
