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W R Finnerty

Publications and source records attributed to W R Finnerty.

At least 37 records · Page 2Linked to original sources
PubMed1979

Cellular lipids of the Legionnaires' disease bacterium.

We qualitatively and quantitatively analyzed the simple and complex lipids of 10 Legionnaires' disease bacteria. The phospholipids in decreasing order of concentration were phosphatidylcholine, phosphatidylethanolamine, cardiolipin, phosphatidylmonomethylethanolamine, phosphatidylglycerol, and phosphatidyldimethylethanolamine. The total phospholipids averaged 96 micromoles per gram dry cell weight. Phospholipid fatty acids were solely branched-chain fatty acids and were, in decreasing order of concentration, iso-C16:0, anteiso-C15:0, anteiso-C17:0, iso-C14:0, iso-C16:1, and an unidentified fatty acid. Neutral lipids identified were free fatty acid, ubiquinone, triglyceride, diglyceride, monoglyceride, and wax ester. Neutral lipid fatty acids consisted predominately of branched-chain fatty acids, normal fatty acids, and a minor unidentified fatty acid. Analysis of the cellular lipids of 10 Legionnaires' disease bacteria revealed an unusual and novel microorganism.

Bacteria↗
PubMed1979

Fine structure of the Legionnaires' disease bacterium. In-vitro and in-vivo studies of four isolates.

We obtained four bacterial isolates from patients with Legionnaires' disease and examined them for in-vitro and in-vivo fine-structure characteristics. All isolates had an outer membrane, cytoplasmic membrane, and intracellular membrane structure. Numerous intracellular inclusions were seen, particularly from in-vivo specimens, and appeared membrane-limited. Fine-structure analysis did not reveal the presence of a definitive peptidoglycan structure. Isolation, purification, and chemical analysis of Legionnaires' disease bacterium pepdoglycan established molar ratios of alanine-glutamic acid and muramic acid-glucosamine. Diaminopimelic acid was absent in the Legionnaires' disease bacterium peptidoglycan. The Kellenberger procedure for fixation appears to be the best method for the fine-structure determination of Legionnaires' disease bacteria.

Alanine↗
PubMed1977

Metabolism of the alkane analogue n-dioctyl ether by Acinetobacter species.

Metabolism of n-dioctyl ether by Acinetobacter species HO1-N resulted in formation of 8-n-octoxy-1-octanoic acid and 2-n-octoxy-1-acetic acid. The 16-carbon ether acid was incorporated into the cellular lipids, whereas the 10-carbon ether acid accumulated in the growth medium. Qualitative and quantitative characteristics of the cellular phospholipids were similar to hexadecane-grown cells. The growth of Acinetobacter on dioctyl ether occurred at the expense of six-carbon atoms of dioctyl ether.

Acetates↗
PubMed1977

Characterization of lysocardiolipin from Acinetobacter sp. HO1-N.

Triacyl-lysocardiolipin (triacyl-LCL) and diacyl-LCL were isolated from Acinetobacter sp. HO1-N, and their structures were determined by chemical, physical, and enzymatic procedures. Deacylation of triacyl-LCL and diacyl-LCL yielded bis-glycerylphosphorylglycerol. Periodate oxidation of both lysolipids was negative. Diglyceride and 2-monoglyceride resulted from the acetic acid hydrolysis of triacyl-LCL, whereas 2-monoglyceride was the sole product obtained from diacyl-LCL. Cardiolipin (CL)-specific phospholipase D treatment of triacyl-LCL yielded lysophosphatidylglycerol and phosphatidic acid. Pancreatic lipase treatment of CL yielded triacyl-LCL and diacyl-LCL. 31P nuclear magnetic resonance spectrometry showed two resonance peaks separated by 40 HZ for CL, two overlapping peaks separated by 14 HZ for triacyl-LCL, and one peak for diacyl-LCL. The proportion of lysocardiolipin increased as a function of cell age, representing 2 to 3% of the total phospholipids in early- and mid-exponential growth, 5 to 7% in late-exponential growth, and 12% in the stationary growth phase.

Acinetobacter↗
PubMed1977

Outer membrane phospholipase A from Acinetobacter sp. HO1-N.

A phospholipase A1 activity that hydrolyzed cardiolipin to triacyl- and diacyl-lysocardiolipin was localized in outer membrane preparations derived from Acinetobacter sp. HO1-N. The specific activity of the enzyme derived from hexadecane-grown cells was 2.5 to 3 times higher than that derived from NBYE-grown cells. An apparent Km of 2.22 mM was determined, although inhibition kinetics resulted at the higher cardiolipin substrate concentrations. Optimal reaction conditions established on metal requirements. Enzyme activity was obligately dependent on Triton X-100 (0.5%) and was inhibited by cationic and anionic detergents. Cardiolipin-specific phospholipase D converted triacyl-lysocardiolipin to lysophosphatidylglycerol and phosphatidic acid. The specific activity of this enzyme was approximately 100 times greater than that reported for other membrane preparations derived from microorganisms.

Acinetobacter↗
PubMed1976

A comparative analysis of the ultrastructure of hydrocarbon-oxidizing micro-organisms.

The ultrastructure of a variety of micro-organisms was compared after growth on hydrocarbon and non-hydrocarbon substrates. Hydrocarbon-grown organisms were characterized by the presence of intracellular electron-transparent inclusions which in many cases appeared membrane-bound. With one exception, non-hydrocarbon-grown organisms did not contain electron-transparent inclusions. Insignificant amounts of poly-beta-hydroxybutyric acid were produced by the hydrocarbon-grown micro-organisms. After growth on hydrocarbons, all the microorganisms had accumulated varying amounts of the respective unmodified hydrocarbon growth substrate.

Acinetobacter↗
PubMed1976

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

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.

Acinetobacter↗
PubMed1976

Characterization of intracytoplasmic hydrocarbon inclusions from the hydrocarbon-oxidizing Acinetobacter species HO1-N.

The ultrastructure of Acinetobacter sp. strain HO1-N grown on hydrocarbon and nonhydrocarbon substrates was compared using thin sections and freeze-etching. Hydrocarbon-grown cells were characterized by the presence of intracytoplasmic membrane-bound hexadecane inclusions. This membrane did not exhibit a typical unit membrane structure but appeared as a monolayer. The freeze-etch technique revealed the internal structure of the hexadecane inclusions and provided evidence for the presence of a smooth-surfaced limiting membrane. Freeze-etching also revealed intracytoplasmic membranes in the hexadecane-grown cells. These ultrastructural modifications were not present in nonhydrocarbon-grown cells. The hexadecane inclusions were isolated from Acinetobacter. Negative-staining of the inclusions revealed electron-transparent vesicles approximating the size of the inclusions seen in whole cells. Freeze-etching of the purified inclusions revealed membrane-bound vesicles. The purified inclusions exhibited a relatively high value of lipid phosphorus to protein. The lipid composition and the electrophoretic banding pattern of the inclusions on sodium dodecyl sulfate-polyacrylamide gels were determined and compared with other membrane fractions (outer membrane and cytoplasmic membrane) previously isolated from this organism.

Acinetobacter↗
PubMed1976

Phospholipid composition and phospholipase A activity of Neisseria gonorrhoeae.

Exponential-phase cells of Neisseria gonorrhaeae 2686 were examined for phospholipid composition and for membrane-associated phospholipase A activity. When cells were harvested by centrifugation, washed, and lyophilized before extraction, approximately 74% of the total phospholipid was phosphatidylethanolamine, 18% was phosphatidylglycerol, 2% was cardiolipin, and 10% was lysophosphatidylethanolamine. However, when cells still suspended in growth medium were extracted, the amount of lysophosphatidylethanolamine decreased to approximately 1% of the phospholipid composition. This suggests that a gonococcal phospholipase A may be activated by conditions encountered during centrifugation and/or lyophilization of cells preceding extraction. Phospholipase A activity associated with cell membranes was assayed by measuring the conversion of tritiated phosphatidylethanolamine to lysophosphatidylethanolamine. Optimal activity was demonstrated in 10% methanol at pH 8.0 to 8.5, in the presence of calcium ions. The activity was both detergent sensitive and thermolabile. Comparisons of gonococcal colony types 1 and 4 showed no significant differences between the two types with respect to either phospholipid content or phospholipase A activity.

Calcium↗
PubMed1975

Microbial assimilation of hydrocarbons. I. The fine-structure of a hydrocarbon oxidizing Acinetobacter sp.

1. The fine-structure analysis of the hydrocarbon oxidizing microorganism, Acinetobacter sp., demonstrated a cytoplasmic modification resulting from growth on paraffinic and olefinic hydrocarbons. 2. Intracytoplasmic hydrocarbon inclusions were documented by electron microscopy with chemical identifications obtained by gas chromatography and X-ray diffraction. 3. These results demonstrate the ability of a microorganism to accumulate hydrocarbon substrates intracellularly which, in turn, indicates the transport across the cell membrane.

Acinetobacter↗
PubMed1975

Microbial assimilation of hydrocarbons. II. Intracytoplasmic membrane induction in Acinetobacter sp.

1. The induction of intracytoplasmic membranes was demonstrated to occur in Acinetobacter sp. when grown on hexadecane, heptadecane, and hexadec-1-ene. 2. Evidence for a physical relationship between the cytoplasmic hydrocarbon "pools" and the intracytoplasmic membranes is presented. 3. The specificity of cytoplasmic pooling of hydrocarbons and the induction of intracytoplasmic membranes was investigated in relationship to hydrocarbon oxidation. 4. These results suggests that both processes are required for the growth of Acinetobacter sp. on hydrocarbons.

Acinetobacter↗
PubMed1975

Comparative analysis of the lipids of Acinetobacter species grown on hexadecane.

A comparative analysis of the cellular and extracellular lipids of Acinetobacter species HO1-N indicated basic physiological differences in hexadecane-grown cells. The cellular lipids obtained from hexadecane-grown cells were characterized by 3- and 18-fold increases in the phospholipid fraction and the mono- and diglyceride fraction, respectively, over that obtained from nutrient broth-yeast extract-grown cells. The cellular-associated pools of hexadecane were shown to comprise approximately 8% of the dry cell weight of hexadecane-grown cells. The extracellular lipids obtained from the culture broths of hexadecane-grown cells were comprised of triglyceride, mono- and diglyceride, free fatty acid, and wax ester. These lipids were either absent or present in minor concentrations in the culture broths of nutrient broth-yeast extract-grown cells. The exponential growth of Acinetobacter sp. on hexadecane was characterized by the significant accumulation of free fatty acid, monoglyceride, and diglyceride in the culture medium. Wax ester was shown to represent a minor portion of the extracellular lipids during the exponential growth phase, appearing in significant proportion only after the culture had entered the stationary phase of growth.

Acinetobacter↗
PubMed1975

Isolation and characterization of an ornithine-containing lipid from Desulfovibrio gigas.

The isolation and characterization of an ornithine-containing lipid obtained from Desulfovibrio gigas are reported. The general structure for this aminolipid is represented by NH2-CH2-(CH)2-CHNH(CO-CH2CH(O-COR2)-R1)-COOH, where R1 represents 3-hydroxy palmitate linked through an amide bond to the alpha-amino group of ornithine, and R2 represents a complex variety of fatty acids esterified to the hydroxyl group of 3-hydroxy palmitate. Fatty acids characterized were n-C14:0 (21%), iso-C14:0 (14%) anteiso-C15:0 (43%), n-C16:0 (2%), n-C18:0 (8%), and n-C 18:1 (11%). The quantitative relationships between aminolipid and phospholipids showed the aminolipid to represent the major polar lipid. Isolation of the cytoplasmic and outer membranes of D. gigas showed the aminolipid to be evenly distributed between both membrane fractions, suggesting a compensatory role in phospholipid-deficient membranes.

Amino Acids↗