Purification and partial characterization of a bacteriocin from Serratia marcescens.

Abstract:

:Bacteriocin JF246 has been purified from mitomycin C-induced Serratia marcescens cells by salt extraction, ammonium sulfate fractionation, and chromatography on QAE-Sephadex and SP-Sephadex. The purified material is homogeneous on polyacrylamide gel electrophoresis in the presence of 2% sodium dodecyl sulfate or 6 m urea. In the absence of these agents, the bacteriocin associates into aggregates which can be dissociated with 0.4 m NaCl. The bacteriocin is probably composed of a single subunit with a molecular weight of 64,000 daltons. Analytical studies show the bacteriocin to be essentially protein in nature containing less than one residue of glucose or phosphorus per 64,000 daltons.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Foulds J

doi

10.1128/JB.110.3.1001-1009.1972

subject

Has Abstract

pub_date

1972-06-01 00:00:00

pages

1001-9

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

110

pub_type

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