Affordable Access

Publisher Website

Microcin 7: Purification and properties

Authors
Publisher
Elsevier Inc.
Publication Date
Volume
119
Issue
2
Identifiers
DOI: 10.1016/s0006-291x(84)80318-6

Abstract

Microcin 7 is an antibiotic peptide, produced and excreted to the culture medium by E. coli strains harboring the plasmid pRYC7. This peptide was extracted from the culture media by adsorbing it on octadecyl silica. It was purified by gel filtration on Sephadex G-25 and reverse phase high performance liquid chromatography. Its amino acid composition is the following: Ala (0.8), Arg (1.9), Asx (1.9), Gly (1.5), Met (0.8) and Thr (0.9). The purified peptide does not react with ninhydrin and it is resistant to carboxypeptidase degradation, indicating that the molecule may be a cyclic or end-blocked oligopeptide.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Microcin 7: purification and properties.

on Biochemical and Biophysical Re... Mar 15, 1984

Gene 6 exonuclease of bacteriophage T7. I. Purific...

on Journal of Biological Chemistr... Jan 10, 1972

Structure and properties of Ni7cluster isomers

on Chemical Physics Letters Jan 01, 1996

Bacteriophage T7-induced endonuclease II. Purifica...

on Journal of Biological Chemistr... Jan 10, 1972
More articles like this..