The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus aureus: II. The Amino Acid Sequences of Tryptic and
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.
Number of Image Pages:
16 (2,556,979 Bytes)
1967-10-25 (October 25, 1967)
Anfinsen, Christian B.
Periodical: Taniuchi, Horoshi, Christian B. Anfinsen, and Ann Sodja. "The Amino Acid Sequence of an Extracellular Nuclease of Staphylococcus
aureus: II. The Amino Acid Sequences of Tryptic and Chymotryptic Peptides." Journal of Biological Chemistry 242, 20 (25
October 1967): 4736-4751. Article. 16 Images.
American Society for Biochemistry and Molecular Biology
Reproduced with permission of the American Society for Biochemistry and Molecular Biology.