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PMID: 132429 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Isolation and characterization of membranes from a hydrocarbon-oxidizing Acinetobacter sp.

Journal of bacteriology ·Vol. 127 ·No. 1 ·1976-07-00 ·Pages 469-80

Scott CC, Makula SR, Finnerty WR

Abstract

Membranes were isolated and purified from nutrient broth-yeast extract- and hexadecane-grown cells of Acinetobacter sp. strain HO1-N. Two membrane fractions were isolated from nutrient broth-yeast extract-grown cells, the cytoplasmic membrane and the outer membrane. In addition to these two membrane fractions, a unique membrane fraction was isolated from hexadecane-grown cells (band 1) and characterized as a lipid-rich, low-density membrane containing high concentrations of hexadecane. The outer membrane preparations of Acinetobacter, obtained from nutrient broth-yeast extract- and hexadecane-grown cells, exhibited a low ratio of lipid phosphorus to protein and contained phospholipase activity and 2-keto-3-deoxyoctulosonic acid. Phosphatidic acid cytidyltransferase, adenosine triphosphatase, and reduced nicotinamide adenine dinucleotide oxidase were recovered almost exclusively in the cytoplasmic membrane fractions. The cytoplasmic membrane fractions contained 20 to 25 polypeptide species on sodium dodecyl sulfate-polyacrylamide gels, and the outer membrane fractions contained 15 to 20 polypeptide species. A major polypeptide species with an apparent molecular weight of approximately 42,000 to 44,000 was found for all outer membrane fractions. The buoyant densities of the cytoplasmic membrane fractions and the outer membrane fractions were closely similar, necessitating their separation by differential centrifugation. Band 1 of hexadecane-grown cells had a ratio of lipid phosphorus to protein that was almost twice that of cytoplasmic membrane and a correspondingly low buoyant density (1.086 g/cm3). Enzyme activities associated with band 1 were identical to those associated with the cytoplasmic membrane. The electrophoretic banding pattern of band 1 was essentially identical to the banding pattern of the cytoplasmic membrane. The phospholipid and neutral lipid compositions of the isolated membrane fractions were determined as qualitatively similar, with significant quantitative differences. The ultrastructure characteristics of the respective membrane fractions were examined by the negative-stain technique.

MeSH Terms
Acinetobacter/metabolism,ultrastructure Adenosine Triphosphatases/metabolism Alkanes/metabolism Bacterial Proteins/analysis Cell Membrane/analysis,enzymology,ultrastructure Cell Wall/analysis,ultrastructure Ketoses/analysis Lipids/analysis Lipopolysaccharides/analysis NADH, NADPH Oxidoreductases/metabolism Nucleotidyltransferases/metabolism Peptides/analysis Phospholipases/metabolism Phospholipids/analysis Phosphorus/analysis Polysaccharides, Bacterial/analysis Subcellular Fractions/analysis Sugar Acids/analysis
Chemicals
Alkanes Bacterial Proteins Ketoses Lipids Lipopolysaccharides Peptides Phospholipids Polysaccharides, Bacterial Sugar Acids Phosphorus NADH, NADPH Oxidoreductases Nucleotidyltransferases Phospholipases Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Scott C C
Makula S R
Finnerty W R
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41 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.127.1.469-480.1976
Published
1976-07-00
Pages
469-80
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC233080
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.127.1.469-480.1976 PMC Full Text View journal details
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