The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus aureus: II. The Amino Acid Sequences of Tryptic and Chymotryptic Peptides

The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus aureus: II. The Amino Acid Sequences of Tryptic and Chymotryptic Peptides

Contributor(s):
Sodja, Ann
Taniuchi, Horoshi
Anfinsen, Christian B. (Christian Boehmer), 1916-1995
Journal of Biological Chemistry
Publication:
American Society for Biochemistry and Molecular Biology, 25 October 1967
Language(s):
English
Format:
Text
Subject(s):
Amino Acid Sequence
Peptides
Micrococcal Nuclease
Research Design
Genre(s):
Archival Materials
Articles
Abstract:
Throughout the late 1960s, the primary concern of Anfinsen's laboratory was to understand the relationship between structure and function in staphylococcal nuclease. Anfinsen chose to study this enzyme because it was relatively small, with only 149 amino acids, and because it appeared to be entirely dependent on noncovalent binding for the maintenance of an ordered catalytically active structure. In this series of three articles, authored by Anfinsen and Taniuchi, but based primarily on research conducted by the latter, the two scientists presented the first analysis of the primary sequence of the enzyme.
Copyright:
This item may be under copyright protection; contact the copyright owner for permission before re-use.
Extent:
16 pages
NLM Unique ID:
101584571X147 (See in Profiles in Science)
Profiles in Science ID:
KKBBKB
Permanent Link:
http://resource.nlm.nih.gov/101584571X147
Archival Collection:
The Christian B. Anfinsen Papers (Profiles in Science)