z-logo
open-access-imgOpen Access
Partial Purification and Some Properties of the Uridine Diphospho- N -Acetylglucosamine-Enolpyruvate Reductase from Staphylococcus epidermidis
Author(s) -
Gary G. Wickus,
Peter A. Rubenstein,
A. D. Warth,
Jack L. Strominger
Publication year - 1973
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.113.1.291-294.1973
Subject(s) - biology , uridine , biochemistry , flavin adenine dinucleotide , enzyme , staphylococcus epidermidis , flavoprotein , cofactor , staphylococcus aureus , microbiology and biotechnology , bacteria , rna , genetics , gene
A method for the partial purification of the uridine diphospho-N -acetylglucosamine-enolpyruvate reductase fromStaphylococcus epidermidis is presented. Some properties of the enzyme, including its dependence on monovalent cation and flavine adenine dinucleotide, are discussed.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom