alpha-Amylase from the Hyperthermophilic Archaebacterium Pyrococcus furiosus

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)