alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus
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)
1993-11-15 (November 15, 1993)
Laderman, Kenneth A.
Anfinsen, Christian B.
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.
American Society for Biochemistry and Molecular Biology
Reproduced with permission of the American Society for Biochemistry and Molecular Biology.