The isolation of arylsulphatase isoenzymes from Pseudomonas aeruginosa

Delisle, Gloria; Milazzo, F. H.

doi:10.1016/0005-2744(70)90258-5

Cited by 23 publications

(14 citation statements)

References 8 publications

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“…MS activity with I? aeruginosa has not been reported previously and is mediated by an enzyme that differs from the aryl- [36], choline- [37] and alkyl- [38] sulphatase activities that have been known for some time. No sulphatase activity of any kind has been demonstrated before in B. cepacia.…”

Section: Discussionmentioning

confidence: 87%

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A novel mucin-sulphatase activity found in Burkholderia cepacia and Pseudomonas aeruginosa

Jansen

Hart

Rhodes

et al. 1999

Journal of Medical Microbiology

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Lung infections due to Burkholderia cepacia and Pseudomonas aeruginosa in patients with cystic fibrosis (CF) are common, are associated with respiratory morbidity and are a cause of mortality. Respiratory mucin in CF patients is highly sulphated, which increases its resistance to bacterial degradation. Desulphation increases the susceptibility of mucin to degradation by bacterial glycosidases and proteinases, and subsequent deglycosylation may facilitate bacterial colonisation by increasing available substrates and binding sites. This study determined whether clinical and environmental strains of B. cepacia and I! aeruginosa had the ability to desulphate mucin. Mucin-sulphatase activity was tested by incubating bacterial cell suspensions with 35S-sulphated mucins purified from LSl74T and HT29-MTX human colon carcinoma cell lines. These mucins were also used to test for differences in substrate specificities. Mucin-sulphatase activity was detected in all nine B. cepacia strains and in four of six I! aeruginosa strains. There was strain variability in the level of mucin-sulphatase activity. Aryl-sulphatase activities of Pseudomonas isolates (determined with methylumbelliferyl sulphate) were c. 20-fold higher than those of B. cepacia strains, and were independent of mucin-sulphatase activity. This is the first report to demonstrate desulphation of mucin by B. cepacia and I! aeruginosa. It is concluded that B. cepacia and I! aeruginosa produce one or more cell-bound glycosulphatase(s), in addition to aryl-sulphatase activity. Mucin-sulphatase activity of B. cepacia and I! aeruginosa may contribute to their association with airway infections in patients with cystic fibrosis.

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Section: Discussionmentioning

confidence: 87%

“…Strains of l? aeruginosa [36] and faecal homogenate from patients with ulcerative colitis were used as positive controls; E. coli K12 and Tris buffer were negative controls. Suspensions of bacterial cells in Tris buffer served to control for autofluorescence of bacterial products.…”

Section: Aryl-sulphatase Assaymentioning

confidence: 99%

A novel mucin-sulphatase activity found in Burkholderia cepacia and Pseudomonas aeruginosa

Jansen

Hart

Rhodes

et al. 1999

Journal of Medical Microbiology

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“…Arylsulfatase a and p were extracted from Pse~idoi~~or~os oer~iginosa and purified as described previously (6). Their separation was achieved by elution from acrylamide gel following electrophoresis (21).…”

Section: Enzytt~ementioning

confidence: 99%

“…Recently we reported the first isolation of two highly purified arylsulfatase isoenzymes from Pseudoionloi~as aeruginosa grown under conditions of sulfate deprivation (6). These isoenzymes were found to be charge isomers, pI 4.85 and pI 4.90 with a molecular weight of about 60 000.…”

Section: Introductionmentioning

confidence: 97%

Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa

Delisle¹,

Milazzo²

1972

Can. J. Microbiol.

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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.

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“…Arylsulfatase (aryl-sulfate sulfohydrolase, EC3.1.6.1) is a class of glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes to hydrolyze arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. Several studies have reported on various arylsulfatases isolated from bacteria such as Klebsiella pneumoniae [9], Salmonella typhimurium [10,11], Serratia marcescens [12], and Pseudomonas aeruginosa [13]. P. carrageenovora arylsulfatase is considerably smaller (36 kDa) than the other bacterial sulfatases, and does not display sequence similarity to any of the sulfatases [14].…”

Section: Introductionmentioning

confidence: 99%

Constitutive overexpression of Pseudoalteromonas carrageenovora arylsulfatase in E. coli fed-batch culture

Kim

Nam

2011

Korean J. Chem. Eng.

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The arylsulfatase gene (astA) from Pseudoalteromonas carrageenovora genome was subcloned into pHCE-IA vector, in which the hyper constitutive expression (HCE) promoter from the D-amino acid aminotransferase (D-AAT) gene of Geobacillus toebii was employed. When the constructed pHCE-AST was introduced into E. coli, the transformant showed the hydrolyzing activity for 4-methylumbelliferyl-sulfate and p-nitrophenyl-sulfate. When the cell was cultured on fermentor containing MaxyBroth-HD medium with 1% glycerol, the enzyme activity reached 12.8 unit/mL. On MaxyBroth-HD medium with 2% glycerol, the cell showed 2.7-fold higher arylsulfatase expression than that with 1% glycerol. The fed-batch cultivation employing MaxyBroth-HD medium and additional feeding of glycerol gave about 143 unit/mL of arylsulfatase at 20 h, which corresponds to 4-fold higher enzyme activity than that of 2% glycerol batch culture. Most of arylsulfatase activity in fed-batch culture was produced in the extracellular medium, whereas the activity in the batch cultures was localized in the periplasmic cell space.

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The isolation of arylsulphatase isoenzymes from Pseudomonas aeruginosa

Cited by 23 publications

References 8 publications

A novel mucin-sulphatase activity found in Burkholderia cepacia and Pseudomonas aeruginosa

A novel mucin-sulphatase activity found in Burkholderia cepacia and Pseudomonas aeruginosa

Characterization of arylsulfatase isoenzymes from Pseudomonas aeruginosa

Constitutive overexpression of Pseudoalteromonas carrageenovora arylsulfatase in E. coli fed-batch culture

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