Title:

alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus

Creator:

Anfinsen, Christian B. (Christian Boehmer), 1916-1995
Uemori, T.
Laderman, Kenneth A.
Kato, I.
Taguchi, Y.
Asada, Kiyozo
Mukai, H.

Date:

15 November 1993

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.

Periodical:

Journal of Biological Chemistry

Publisher:

American Society for Biochemistry and Molecular Biology

Location:

Box: 28. Folder: 7

Rights:

Reproduced with permission of the American Society for Biochemistry and Molecular Biology. and http://www.jbc.org/

Genre:

Articles

Subject:

alpha-Amylases, Pyrococcus furiosus, Recombinant Proteins, and Amino Acid Sequence

Format:

Text

Extent:

6 pages

Language:

English

Legacy Source Citation:

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.. Journal of Biological Chemistry

Legacy ID:

KKBBKP

NLM ID:

101584571X158

Profiles Collection:

The Christian B. Anfinsen Papers

Shareable Link:

https://profiles.nlm.nih.gov/101584571X158

Story Section:

Interferon and Thermophilic Bacteria, 1973-1995