A <i>p</i>-nitrophenyl α-galactoside hydrolase from <i>Pseudomonas atlantica</i>. Localization of the enzyme

Day, Donal F.; Gomersall, M.; Yaphe, W.

doi:10.1139/m75-219

Cited by 8 publications

(4 citation statements)

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“…On the other hand, very few reports on glycosidases from gram-negative bacteria, with the exception of Escherichia coli (24) and Pseudomonas species (2,8), have been published. A Bacteroides amylase was recently studied by McWethy and Hartman (12).…”

Section: Discussionmentioning

confidence: 99%

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Formation of glycosidases in batch and continuous culture of Bacteroides fragilis

Berg¹,

Nord²,

Wadström³

1978

Appl Environ Microbiol

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Nine strains of Bacteroides fragilis were cultivated in stirred fermentors and tested for their ability to produce glycosidases. B. fragilis subsp. vulgatus B70 was used for optimizing the production of glycosidases. The highest bacterial yield was obtained in proteose peptone-yeast extract medium. The optimum pH for maximal bacterial yield was 7.0, and the optimum temperature for growth was 37°C. The formation of glycosidases was optimal between pH 6.5 and 7.5, and the optimum temperature for synthesis of glycosidases was between 33 and 370C. Culture under controlled conditions in fermentors gave more reproducible production of glycosidases than static cultures in bottles. The strain was also grown in continuous culture at a dilution rate of 0.1 liter/h at pH 7.0 and 370C with a yield of 2.0 mg of dry weight per ml in the complex medium. The formation of glvcosidases remained constant during the entire continuous process.

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Section: Discussionmentioning

confidence: 99%

“…fragilis produced glycosidases both during the logarithmic and the lytic phases. These enzymes are probably released into the medium upon cell lysis, since most glycosidases in gramnegative bacteria are known to be cytoplasm located (2,8,18,24).…”

Section: Formation Of B Fragilis Glycosidasesmentioning

confidence: 99%

Formation of glycosidases in batch and continuous culture of Bacteroides fragilis

Berg¹,

Nord²,

Wadström³

1978

Appl Environ Microbiol

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“…This reagent is therefore useful in identifying proteins that are external, or are attached, to the outer surface of the plasma membrane (30). It has been used to prove the surface location of the (3-galactoside permease of E. coli (30), the sulfate-binding protein of Salmonella typhimurium (30), and the a-galactosidase of Pseudomonas atlantica (8). Diazo-NDS inactivated the SOD activity of cell-free extracts ofE.…”

Section: Methodsmentioning

confidence: 99%

Intracellular localization of the superoxide dismutases of Escherichia coli: a reevaluation

Britton¹,

Fridovich²

1977

J Bacteriol

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All of the superoxide dismutase isozymes ofEscherichia coli have been shown to occur in the cell matrix, and none have been found in the periplasm. This was the case with both E. coli B and E. coli K-12, whether grown on a low phosphate medium or on a Trypticase soy-yeast extract medium. Alkaline phosphatase was used as a marker of the periplasm; adenosine deaminase and glucose 6-phosphate dehydrogenase were used as matrix markers, and consistent results were obtained by osmotic shock, spheroplast formation, and use of a diazonium salt that penetrates the periplasm but cannot cross the plasma membrane. A previous report that the iron-containing superoxide dismutase of E. coli is a periplasmic enzyme is now seen to have been in error.

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“…Internal enzymes are protected against NDS action by the cytoplasmic membrane (Day & Ingram, 1971 ;Day et al, 1975). In P. aeruginosa K, NDS led to a considerably inactivated ChE, as well as 5'-nucleotidase and ATPase, without affecting 3-phosphoglycerate kinase activity.…”

Section: Discussionmentioning

confidence: 99%

Localization of Cholinesterase in Pseudomonas aeruginosa Strain K

Garber

Nachshon

1980

Microbiology

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The inducible cholinesterase of Pseudomonas aeruginosa strain K (ATCC 25 102) degraded propionylcholine, acetylthiocholine, acetylcholine and acetyl-P-methylcholine at a high rate and butyrylcholine and succinylcholine at very low rates. The localization of the enzyme in the periplasmic space was indicated by a similar rate of acetylcholine degradation by intact cells or their extracts, by release of cholinesterase together with alkaline phosphatase into the culture medium during cell growth in a low phosphate-containing medium, by liberation of cholinesterase and alkaline phosphatase during lysozyme-induced conversion of cells to spheroplasts and by freezing and thawing. Treatment of cells with diazo-7-amino-l,3-naphthalenedisulphonic acid, which inactivates surface-located enzymes, abolished most of the cholinesterase and 5'-nucleotidase activities.

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A p-nitrophenyl α-galactoside hydrolase from Pseudomonas atlantica. Localization of the enzyme

Cited by 8 publications

References 0 publications

Formation of glycosidases in batch and continuous culture of Bacteroides fragilis

Formation of glycosidases in batch and continuous culture of Bacteroides fragilis

Intracellular localization of the superoxide dismutases of Escherichia coli: a reevaluation

Localization of Cholinesterase in Pseudomonas aeruginosa Strain K

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