Verstärkung der Katalasewirkung in Hefezellen.

Euler, Hans v.; Blix, Ragnar

doi:10.1515/bchm2.1919.105.3-4.83

Cited by 29 publications

(6 citation statements)

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“…3). A similar phenomenon was observed for catalase activity in distiller's yeast (7). Aryl sulfatase is quite stable at elevated temperatures; however, after the first 5 min of heat treatment, aryl sulfatase activity decreased at a rate parallel to the loss of activity in conidia whose permeability barrier was previously destroyed with chloroform.…”

Section: Methodssupporting

confidence: 72%

Location of Aryl Sulfatase in Conidia and Young Mycelia of Neurospora crassa

Scott

Metzenberg

1970

J Bacteriol

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Aryl sulfatase (arylsulfate sulfohydrolase, EC 3.1.6.1) was found to have multiple locations in Neurospora conidia. Some enzyme activity remained in the supernatant when a spore suspension was centrifuged or filtered. Part of the cell-bound activity could be detected by adding the assay ingredients to a suspension of intact spores (patent enzyme), and additional activity was only detectable when the spores were first treated to destroy their permeability barriers (cryptic enzyme). Such treatments include: disruption with an X-press, brief rinsing with chloroform or acetone, incubation at 60 C for 5 min, and incubation with phenethyl alcohol, nystatin, or ascosin. Part of the patent aryl sulfatase was inactivated by briefly acid treating the intact spores (no loss of conidial viability). This enzyme was considered to have a cell surface location. Some enzyme was acid-resistant in intact spores, but all of the enzyme was acid-sensitive in spores whose permeability barriers had been disrupted. The p H dependence, kinetic properties, and p -nitrophenyl sulfate uptake were investigated in acid-treated conidia. No aryl sulfatase was detected in ascospores. Young mycelia contained more aryl sulfatase than did conidia, but little, if any, was secreted into the growth medium. Cryptic activity was demonstrated in young mycelia by brief chloroform treatment or by rinsing the cells with 0.1 m acetate buffer. Enzyme activity in young mycelia was completely labile to acid treatment, as was cell viability.

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Section: Methodssupporting

confidence: 72%

Location of Aryl Sulfatase in Conidia and Young Mycelia of Neurospora crassa

Scott

Metzenberg

1970

J Bacteriol

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“…The L forms lyse to a large extent when transferred to dilute buffers, whereas normal bacteria are highly resistant to osmotic forces. This could explain the higher catalase activity of the L forms, since it is known that a degradation of the structure of microbial cells enhances their catalase activity (Euler and Blix, 1919; Herbert and Pinsent, 1948;Preiss, 1959). The low catalase activity of one of the L forms, L 9, may also be explained by lytic effects.…”

Section: Discussionmentioning

confidence: 97%

“…Pure catalase has a turnover number of about 107 molecules per min per molecule of catalase (Sumner and Somers, 1947;Herbert and Pinsent, 1948). However, catalase molecules inside intact cells seem to split H202 about ten times slower (Euler and Blix, 1919;Herbert and Pinsent, 1948), and are thus characterized by a turnover number of about 106. The average diameter of PPLO cells is approximately 0.4 ,u (Bartmann and Hopken, 1955;Weibull and Lundin, 1962).…”

Section: Discussionmentioning

confidence: 99%

Occurrence of Catalase in Pleuropneumonia-Like Organisms and Bacterial L Forms

Weibull¹,

Hammarberg²

1962

J Bacteriol

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The catalase activity of six pleuropneumonia-like organisms (PPLO), four stable Proteus L forms, and four normal strains of Proteus mirabilis was determined quantitatively. The PPLO (strains of the species Mycoplasma agalactiae, hominis, laidlawii, mycoides, and strains isolated from tissue cultures) exhibited no measurable catalase activity. The L forms decomposed H202 approximately ten times as rapidly as the normal bacteria from which they were derived. Reports on the catalase activity of p)leuropneumonia-like organisms (PPLO) are confficting. Lecce and Morton (1954) stated that this enzyme is present in the PPLO strain named Campo, and Rodwell and Rodwell (1954) reported its presence in the organism of bovine pleuropneumonia. Freundt (1958) was unable to confirm these observations. Kandler and Kandler (1955) found no catalase in seven saprophytic PPLO strains and one strain isolated from mice. With the exception of the study by Rodwell and Rodwell, the investigations mentioned above were performed by means of qualitative tests To obtain more precise information on the catalase activity of PPLO, the present authors determined the catalase activity of several strains quantitatively. The catalase of four stable Proteus L forms was measured to plrovide a comparison. The activity of the normal bacteria

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“…They are of the opinion that this may result from the destruction of harmful soil organisms or be a direct physicalchemical effect. Euler and Blix (1919) found that low concentrations of certain protoplasmic poisons would considerably accelerate the catalase activity of yeast cells.…”

Section: Resultsmentioning

confidence: 99%

The Effect of Certain Chemicals on the Catalase Activity in Plants

Landon

1934

American Journal of Botany

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The catalase activity of plant tissues fluctuates with changes in their metabolic activity or physiological condition. The measurement of these fluctuations has been used as a means of ascertaining the response of plants to various treatments. Heinicke (1928) states that despite the fact that nothing definite is known as to the metabolic role of catalase, the measurement of its activity is a reliable and sensitive index to changes occurring in the internal condition of plants.The studies reported in this paper were made for the purpose of determining the effects of several chemicals of known herbicidal value, and some related compounds, on the catalase activity of living plants and plant-tissue preparations. The information is of interest, as there is little mention in the literature concerning the effect of the chemicals studied on catalase activity. Some improvements in the technique of making catalase determinations are also described. EXPERIMENTALMaterials. As the investigation was conducted during the winter months, it was necessary to work with a species of plant adapted to indoor cultivation. Cabbage was used, as it grows well in the greenhouse and has leaves of such size that sampling causes a minimum of shock and injury to the plant. The plants, Copenhagen Market variety, were grown in six-inch pots from one well-mixed lot of seed and were selected for uniformity in age, size, and apparent vigor.Watering was controlled by giving each plant 150 cc. of tap water at about the same time each day. Plants selected and handled as described were found to have approximately the same initial catalase activity.Cabbage leaf tissue is fairly homogeneous as to catalase activity. Samples collected 24 hours apart from 25 untreated plants over a period of several weeks showed a maximum difference in catalase activity of five per cent.Chemicals. The chemicals used were in aqueous solutions of 0.01, 0.1, and 1.0 molar concentration. The ammonium sulfocyanate, ethylene oxide, diethylene oxide, propylene oxide, and sodium chlorate were of technical grade, while the thiourea and sodium arsenite were of CiP, quality. Some

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Verstärkung der Katalasewirkung in Hefezellen.

Cited by 29 publications

References 0 publications

Location of Aryl Sulfatase in Conidia and Young Mycelia of Neurospora crassa

Location of Aryl Sulfatase in Conidia and Young Mycelia of Neurospora crassa

Occurrence of Catalase in Pleuropneumonia-Like Organisms and Bacterial L Forms

The Effect of Certain Chemicals on the Catalase Activity in Plants

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