15 results on '"F. H. Milazzo"'
Search Results
2. The extraction and analysis of lipopolysaccharides from Pseudomonas aeruginosa strain PAO, and three rough mutants
- Author
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L. C. Chan, Andrew M. Kropinski, and F. H. Milazzo
- Subjects
Lipopolysaccharides ,Chemical Phenomena ,Lipopolysaccharide ,Immunology ,Mutant ,Virulence ,Biology ,Polysaccharide ,medicine.disease_cause ,Rhamnose ,Applied Microbiology and Biotechnology ,Microbiology ,chemistry.chemical_compound ,Genetics ,medicine ,Molecular Biology ,chemistry.chemical_classification ,Autoagglutination ,Strain (chemistry) ,Pseudomonas aeruginosa ,Polysaccharides, Bacterial ,General Medicine ,Chemistry ,Glucose ,Lipid A ,chemistry ,Mutation ,Acriflavine - Abstract
Three spontaneously arising rough mutants of Pseudomonas aeruginosa have been isolated by selection for resistance to virulent lipopolysaccharide (LPS) specific bacteriophages. In addition, the first phages specific for rough mutants of P. aeruginosa were isolated. Using these phage and autoagglutination patterns in 4% NaCl and acriflavine, these mutants could be clearly distinguished from the wild-type strain and each other. Chemical analysis of the LPS together with chromatographic resolution of the polysaccharide moieties showed alterations in both O-specific side chains and core regions.
- Published
- 1979
3. Arylsulfatase in Salmonella typhimurium: detection and influence of carbon source and tyramine on its synthesis
- Author
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M J Henderson and F H Milazzo
- Subjects
Salmonella typhimurium ,Diauxie ,Carbohydrates ,Biological Transport, Active ,Tyramine ,Microbiology ,Ammonium Chloride ,chemistry.chemical_compound ,Hydrolysis ,Methionine ,Cyclic AMP ,Glycerol ,Cysteine ,Molecular Biology ,Arylsulfatases ,chemistry.chemical_classification ,Growth medium ,biology ,Sulfates ,Substrate (chemistry) ,Enzyme ,chemistry ,Biochemistry ,biology.protein ,Sulfatases ,Arylsulfatase ,Research Article - Abstract
Arylsulfatase synthesis was shown to occur in Salmonella typhimurium LT2. The enzyme had a molecular weight of approximately 50,000 and was separated into five forms by isoelectrofocusing. The optimal pH for substrate hydrolysis was pH 6.7, with Michaelis constants for nitrocatechol sulfate and nitrophenyl sulfate being 4.1 and 7.9 mM, respectively. Enzyme synthesis was strongly influenced by the presence of tyramine in the growth medium. The uptake of [14C]tyramine and arylsulfatase synthesis were initiated during the second phase of a diauxie growth response, when the organism was cultured with different carbon sources. Adenosine 3',5'-cyclic monophosphoric acid enhanced the uptake of tyramine and the levels of arylsulfatase synthesized. However, the addition of glucose and glycerol to organisms actively transporting tyramine and synthesizing enzyme caused a rapid inhibition of both of these processes. This inhibition was not reversed by adding adenosine 3',5'-cyclic monophosphoric acid. The results suggest that the effect of the carbon source on tyramine transport and arylsulfatase synthesis may be explained in terms of inducer exclusion.
- Published
- 1979
4. Pseudomonas aeruginosa lipopolysaccharide: an uncoupler of mitochondrial oxidative phosphorylation
- Author
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G. Gordon Greer and F. H. Milazzo
- Subjects
Lipopolysaccharides ,Lipopolysaccharide ,Immunology ,Malates ,Antimycin A ,Mitochondria, Liver ,Ascorbic Acid ,Oxidative phosphorylation ,Atractyloside ,Mitochondrion ,Biology ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Microbiology ,Oxidative Phosphorylation ,chemistry.chemical_compound ,Oxygen Consumption ,Tetramethylphenylenediamine ,Glutamates ,Rotenone ,Genetics ,medicine ,Animals ,Molecular Biology ,Uncoupling Agents ,Pseudomonas aeruginosa ,Substrate (chemistry) ,Succinates ,General Medicine ,Oxygen uptake ,Rats ,Adenosine Diphosphate ,chemistry ,Biochemistry ,Respiratory control ,Dinitrophenols - Abstract
The addition of Pseudomonas aeruginosa KCIIR LPS to respiring mitochondria stimulated the rate of substrate oxidation, reduced the respiratory control ratio, stimulated oxygen uptake in state 4, and released the inhibition imposed upon state 3 by atractyloside. It was concluded that LPS acted as an uncoupler of oxidative phosphorylation and that it produced effects similar to those observed with the classical uncoupler 2,4-dinitrophenol.
- Published
- 1975
5. A STUDY OF SOME ASPECTS OF SULFUR METABOLISM IN THE WOOD-ROTTING BASIDIOMYCETE, FOMES GEOTROPUS
- Author
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F. H. Milazzo and G. J. Lougheed
- Subjects
Sulfide ,Immunology ,Sulfur metabolism ,chemistry.chemical_element ,In Vitro Techniques ,Applied Microbiology and Biotechnology ,Microbiology ,chemistry.chemical_compound ,Methionine ,Sulfite ,Sodium sulfate ,Genetics ,Organic chemistry ,Fomes ,Sulfate ,Molecular Biology ,Thiosulfate ,chemistry.chemical_classification ,biology ,Basidiomycota ,General Medicine ,biology.organism_classification ,Sulfur ,chemistry ,Cystine - Abstract
The requirement of an inorganic sulfur source for the growth of Fomes geotropus was demonstrated. Inorganic sulfate supported growth to a greater extent than the other more reduced forms of sulfur: sulfite, thiosulfate, sulfide, and taurine. The presence of a sulfate-activating mechanism involving the active sulfate intermediate 3′-phospho-adenosine-5′-phosphosulfate was indicated. In addition, study of the uptake and incorporation of radioactive sodium sulfate revealed that inorganic sulfur was assimilated into the organic sulfur compounds methionine and cyst(e)ine.
- Published
- 1965
6. Arylsulfatase multiplicity in Proteus rettgeri
- Author
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F. H. Milazzo and J. W. Fitzgerald
- Subjects
Electrophoresis ,Paper ,Immunology ,Streptomycin Sulfate ,Catechols ,Paper electrophoresis ,Acetates ,Sodium Chloride ,Biology ,Vibration ,Applied Microbiology and Biotechnology ,Microbiology ,Chromatography, DEAE-Cellulose ,Phosphates ,Nitrophenols ,Genetics ,Ultrasonics ,Molecular Biology ,Cyanides ,Chromatography ,Cell-Free System ,Sulfates ,Sulfatase ,Sodium ,General Medicine ,Proteus ,Multiple species ,Enzyme assay ,Biochemistry ,Spectrophotometry ,Streptomycin ,biology.protein ,Sulfatases ,Proteus rettgeri ,Arylsulfatase - Abstract
Multiple electrophoretic species of arylsulfatase were demonstrated in sonicates of Proteus rettgeri by paper electrophoresis. Subsequent treatment of the sonicates with streptomycin sulfate and DEAE-cellulose chromatography resolved enzyme activity into four fractions. Electrophoretic examination of each chromatographic fraction revealed sulfatase heterogeneity comparable to that of the initial extract. These electrophoretic components differed in their general response to a number of arylsulfatase inhibitors. The results are discussed in relation to the finding of multiple species of arylsulfatase in other biological systems.
- Published
- 1970
7. Immunoglobulin A proteases in gram-negative bacteria isolated from human urinary tract infections
- Author
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F H Milazzo and G J Delisle
- Subjects
Immunoglobulin A ,Proteases ,Gram-negative bacteria ,Myeloma protein ,Immunology ,Immunoelectrophoresis ,Microbiology ,Species Specificity ,Cricetinae ,Gram-Negative Bacteria ,medicine ,Animals ,Humans ,Polyacrylamide gel electrophoresis ,biology ,medicine.diagnostic_test ,Serine Endopeptidases ,biology.organism_classification ,Molecular biology ,Molecular Weight ,Myeloma Proteins ,Infectious Diseases ,Urinary Tract Infections ,biology.protein ,Colostrum ,Parasitology ,Bacteria ,Peptide Hydrolases ,Research Article - Abstract
Several strains of gram-negative bacteria (seven genera, eight species) isolated from patients with urinary tract infections were found to hydrolyze myeloma immunoglobulin A (IgA) protein. Human IgG and IgM and colostrum IgA were not degraded by these organisms. Examination of cleavage digests showed two fragments of different electrophoretic mobilities, with antigenic reactivity and sodium dodecyl sulfate polyacrylamide gel electrophoresis profiles consistent with their identification as Fc and Fab components. The immunoelectrophoresis patterns of cleavage digests suggested that the proteases responsible for this hydrolysis may be dissimilar in the specificity of their IgA cleavage sites.
- Published
- 1984
8. AN ARYLSULFATASE IN THE WOOD-ROTTING BASIDIOMYCETE, FOMES GEOTROPUS
- Author
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Gloria J. Lougheed and F. H. Milazzo
- Subjects
biology ,Botany ,biology.protein ,Fomes ,Plant Science ,biology.organism_classification ,Arylsulfatase - Published
- 1967
9. The nature of Pseudomonas aeruginosa strain PAO bacteriophage receptors
- Author
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Ken F. Jarrell, F. H. Milazzo, Lora Chan, and Andrew M. Kropinski
- Subjects
Lipopolysaccharides ,Lipopolysaccharide ,viruses ,Immunology ,Viral Plaque Assay ,Flagellum ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Microbiology ,Pilus ,Neutralization ,Bacteriophage ,chemistry.chemical_compound ,Neutralization Tests ,Genetics ,medicine ,Bacteriophages ,Receptor ,Molecular Biology ,Strain (chemistry) ,biology ,Pseudomonas aeruginosa ,Polysaccharides, Bacterial ,General Medicine ,biology.organism_classification ,Kinetics ,chemistry ,Genes ,Mutation - Abstract
Receptors for phages specific to Pseudomonas aeruginosa strain PAO were studied. Phages 16, 44, 109, F8, and PBI are lipopolysaccharide (LPS) specific as shown by neutralization tests. The PhI50's of the LPS, adsorption rate constants with strain PAO and the plaque morphologies of these five phages were quite similar. Phages 1214 and 7 also appear to be LPS-specific on the basis of host–range studies. Phage 73 is pilus-specific, while phages 21 and 68 fall into a group which does not attach to pili, flagella, or LPS. A theoretical approach to the interpretation of phage–cell interactions is presented.
- Published
- 1977
10. Pseudomonas aeruginosa lipopolysaccharide: factors influencing toxicity for isolated mitochondria and endotoxin properties
- Author
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F. H. Milazzo and G. Gordon Greer
- Subjects
Lipopolysaccharides ,Lysis ,Lipopolysaccharide ,Immunology ,Mitochondria, Liver ,Biology ,Bacterial growth ,Mitochondrion ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Microbiology ,chemistry.chemical_compound ,Mice ,Oxygen Consumption ,Arachnida ,Genetics ,medicine ,Animals ,Molecular Biology ,Isolated mitochondria ,Pseudomonas aeruginosa ,Polysaccharides, Bacterial ,Temperature ,General Medicine ,biology.organism_classification ,Culture Media ,Rats ,chemistry ,Limulus ,Toxicity ,Rabbits ,Shwartzman Phenomenon - Abstract
In the present study Pseudomonas aeruginosa lipopolysaccharide (LPS) exhibited the following endotoxin properties: (1) toxicity for mice; (2) gelation of the Limulus lysate; (3) induction of a localized Shwartzman reaction in the skin of rabbits, and (4) anticomplementary activity.Differences in LPS toxicity as measured with the rat liver mitochondrial assay system were found to be related to the nature of the bacterial growth media, the functional integrity of mitochondria, and the time and temperature of mitochondrial assay. The significance of these findings to P. aeruginosa infections is discussed, and it is concluded that LPS is a factor of importance.
- Published
- 1976
11. The effect of some cultural conditions on the arylsulfatase of Proteus rettgeri
- Author
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F. H. Milazzo and J. W. Fitzgerald
- Subjects
education ,Immunology ,chemistry.chemical_element ,Applied Microbiology and Biotechnology ,Microbiology ,Nitrophenols ,chemistry.chemical_compound ,Genetics ,Sulfate ,Molecular Biology ,chemistry.chemical_classification ,Methionine ,biology ,Sulfates ,Temperature ,General Medicine ,Hydrogen-Ion Concentration ,Proteus ,Sulfur ,Enzyme assay ,Culture Media ,Enzyme ,chemistry ,Biochemistry ,biology.protein ,Sulfatases ,Arylsulfatase ,Proteus rettgeri - Abstract
The influence of temperature, pH, and sulfur source on arylsulfatase formation in P. rettgeri was investigated. The highest level of enzyme activity was found when the organism was grown at 28 °C in a glycerol–salts medium (pH 7.0) containing 2.7 mM methionine. Low levels of enzyme activity were found when the organism was grown in the presence of 0.8 and 1.5 mM sulfate but 3.0 and 9.0 mM sulfate repressed enzyme formation.Conditions optimal for the formation of enzyme active against p-nitrophenol sulfate were not identical with those optimal for formation of enzyme active against nitrocatechol sulfate.The findings of this work are compared to similar findings in other bacterial systems.
- Published
- 1967
12. A study of arylsulfatase activity in Proteus rettgeri
- Author
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J. W. Fitzgerald and F. H. Milazzo
- Subjects
Arylsulfatase activity ,Immunology ,Catechols ,Acetates ,Applied Microbiology and Biotechnology ,Microbiology ,Phosphates ,Nitrophenols ,chemistry.chemical_compound ,mental disorders ,Genetics ,Sulfate ,Molecular Biology ,Cyanides ,biology ,Strain (chemistry) ,Sulfates ,Temperature ,General Medicine ,Hydrogen-Ion Concentration ,Proteus ,Biochemistry ,chemistry ,Spectrophotometry ,biology.protein ,Sulfatases ,Arylsulfatase ,Proteus rettgeri - Abstract
Arylsulfatase was detected in a strain of Froteus rettgeri using two substrates, nitrocatechol sulfate (NCS) and nitrophenyl sulfate (NTS). Activity was found when the organism was grown in a chemically defined medium with methionine as the only added source of sulfur. No activity was demonstrated when sulfate was substituted for methionine in the growth medium.Maximum hydrolysis of NCS occurred at pH 6.7 in 0.15 M phosphate buffer at 37 °C and maximum hydrolysis of NPS at pH 8.3 in 0.75 M Tris–acetate buffer at 34.5 °C.Sodium cyanide (10−2 M) inhibited hydrolysis of both substrates and sodium sulfate (10−2 M) inhibited hydrolysis of NCS but not NPS. With sodium dihydrogen phosphate (10−2 M) there was increased hydrolysis of NCS and inhibition of NPS hydrolysis.The sulfatase activity in P. rettgeri is compared with that reported in other bacterial systems.
- Published
- 1966
13. Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa
- Author
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G J Delisle and F H Milazzo
- Subjects
Immunology ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Microbiology ,Isozyme ,Chromatography, DEAE-Cellulose ,Nitrophenols ,Genetics ,medicine ,Molecular Biology ,chemistry.chemical_classification ,Ions ,biology ,Pseudomonas aeruginosa ,Hydrolysis ,Pseudomonas ,Temperature ,Proteins ,General Medicine ,Arylsulfatases ,Hydrogen-Ion Concentration ,biology.organism_classification ,Chromatography, Ion Exchange ,Electrophoresis, Disc ,carbohydrates (lipids) ,Isoenzymes ,enzymes and coenzymes (carbohydrates) ,Kinetics ,Enzyme ,Biochemistry ,chemistry ,Spectrophotometry ,biology.protein ,Sulfatases ,Arylsulfatase - Abstract
A method is described for the separation and isolation of two electrophoretically distinct arylsulfatases (arylsulfatase EC.3.1.6.1) from Pseudomonas aeruginosa.Characterization of the enzymes revealed that they were type I arylsulfatases, with similar kinetic properties. They differed, however, in respect to charge, pH optima for substrate hydrolysis, and activation by anions. In addition, the enzymes displayed dual pH optima curves with both substrates used and the curious property of a shift in pH optima with varied p-nitrophenyl sulfate concentrations.
- Published
- 1972
14. Susceptibility of lipopolysaccharide-defective mutants of Pseudomonas aeruginosa strain PAO to dyes, detergents, and antibiotics
- Author
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Andrew M. Kropinski, L. C. Chan, and F. H. Milazzo
- Subjects
Lipopolysaccharides ,medicine.drug_class ,Polymyxin ,Detergents ,Antibiotics ,Microbial Sensitivity Tests ,Biology ,medicine.disease_cause ,Microbiology ,Surface-Active Agents ,Benzalkonium chloride ,chemistry.chemical_compound ,Ampicillin ,medicine ,Pharmacology (medical) ,Coloring Agents ,Edetic Acid ,Pharmacology ,Pseudomonas aeruginosa ,Cell Membrane ,Anti-Bacterial Agents ,Penicillin ,Infectious Diseases ,chemistry ,Mutation ,Acriflavine ,Muramidase ,Lysozyme ,Research Article ,medicine.drug - Abstract
Lipopolysaccharide-defective mutants of Pseudomonas aeruginosa strain PAO have been isolated on the basis of their resistance to lipopolysaccharide-specific bacteriophages. These mutants have been differentiated by their agglutination in NaCl and acriflavine, phage sensitivity, and chemical analysis of the lipopolysaccharides. The susceptibility of the wild-type strain and four mutants to a series of twenty-six agents, including dyes, detergents, antibiotics, and lysozyme, was examined. The roughest mutant (AK-43) exhibited increased susceptibility to sodium deoxycholate, hexadecylpyridinium chloride, benzalkonium chloride, ampicillin, penicillin G, erythromycin, colymycin, and polymyxin B. The role of cell envelope fractions in antibiotic resistance in P. aeruginosa is discussed.
15. Spontaneous release of lipopolysaccharide by Pseudomonas aeruginosa
- Author
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Andrew M. Kropinski, J Kuzio, F. H. Milazzo, and J E Cadieux
- Subjects
Lipopolysaccharides ,Lipopolysaccharide ,Sodium ,chemistry.chemical_element ,Hemolysis Inhibition ,Biology ,medicine.disease_cause ,Polysaccharide ,Microbiology ,Neutralization ,chemistry.chemical_compound ,medicine ,Hexose ,Molecular Biology ,chemistry.chemical_classification ,Pseudomonas aeruginosa ,Endotoxins ,Electrophoresis ,Biochemistry ,chemistry ,Chromatography, Gel ,Receptors, Virus ,Electrophoresis, Polyacrylamide Gel ,Adsorption ,Research Article - Abstract
Pseudomonas aeruginosa PAO grown in glucose mineral salts medium released lipopolysaccharide which was chemically and immunologically similar to the cellular lipopolysaccharide. In addition, it possessed identical phage E79-inactivating properties. Through neutralization of phage activity and hemolysis inhibition assays, the organism was found to liberate lipopolysaccharide at a constant rate during log-phase growth equivalent to 1.3 to 2.2 ng/10(8) cells over a growth temperature range of 25 to 42 degrees C. At 19 degrees C, a lipopolysaccharide was released which was deficient in phage-inactivating activity but retained its immunological properties. Chemical analysis of lipopolysaccharide extracted from cells grown at 19 degrees C showed a deficiency in the O-side-chain component fucosamine. Gel exclusion chromatography of the polysaccharide fraction derived from lipopolysaccharide isolated from cells grown at 19 degrees C exhibited a decreased content of side-chain polysaccharide as well as a difference in the hexosamine:hexose ratio. The results of sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis confirmed these results as well as establishing that an essentially normal distribution of side-chain repeating unit lengths were to be found in the 19 degrees C preparation. These results suggest a decrease in the frequency of capping R-form lipopolysaccharide at 19 degrees C.
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