Ionospheric Recorders and Sporadic E

Thomas, J. A.; Svenson, A. N.; Brown, HE

doi:10.1071/ph560159

Cited by 12 publications

(3 citation statements)

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“…(a) the decrease in the viscosity of a CM-cellulose solution (Wood, 1971); (b) the appearance of reducing sugars in a solution of CM-cellulose. In the viscometric method it was found that, under the conditions of the assay, the plot of rate of increase of the reciprocal of the viscosity against the enzyme concentration was linear up to at least a value of 0.027min-1 (Thomas, 1956). A value of 0.020min-' was found for 1.0ml of the 20-80 %-satd.-(NH4)2SO4 fraction diluted 2500-fold, and this was chosen as the unit of activity.…”

Section: Methodsmentioning

confidence: 99%

The purification and properties of the C1 component of Trichoderma koningii cellulase

Wood¹,

McCrae²

1972

Biochemical Journal

219

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1. The C(1) component that was isolated from a Trichoderma koningii cellulase preparation (Wood, 1968) by chromatography on DEAE-Sephadex with a salt gradient was still associated with a trace of CM-cellulase activity (determined by reducing-sugar and viscometric methods). 2. Further chromatography on DEAE-Sephadex, with a pH gradient instead of a salt gradient, provided a C(1) component that could still produce reducing sugars from a solution of CM-cellulose (to a very limited extent), but which could no longer decrease the viscosity (i.e. under the assay conditions employed). 3. No evidence for the non-identity of C(1) component and the trace of CM-cellulase activity could be found when electrofocusing was done in a stabilized pH gradient covering three pH units (pH3-6) or, alternatively, only 0.5 pH unit (pH3.72-4.25). 4. The two protein peaks that were separated by electrofocusing in carrier ampholytes covering only 0.5 pH unit (isoelectric pH values of 3.80 and 3.95) were shown to be isoenzymes of the C(1) component: they differed in the extent to which they were associated with carbohydrate (9% and 33%). 5. The purified C(1) component had little ability to attack CM-cellulose or highly ordered forms of cellulose, but degraded phosphoric acid-swollen cellulose readily: cellobiose was the principal product of the hydrolysis (97%). 6. Dewaxed cotton fibre was degraded to the extent of 15% when exposed to high concentrations of C(1) component over a prolonged period: cellobiose was again the principal sugar present in the supernatant (96%). 7. Cellotetraose and cellohexaose were hydrolysed almost exclusively to cellobiose. 8. Evidence indicates that the C(1) component is a beta-1,4-glucan cellobiosylhydrolase.

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Section: Methodsmentioning

confidence: 99%

The purification and properties of the C1 component of Trichoderma koningii cellulase

Wood¹,

McCrae²

1972

Biochemical Journal

219

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“…Jermyn, 1957) would be more significant but the fractionation experiments themselves do not allow any direct conclusions in this respect. It is very likely, however, that the polysaccharase components of both A. oryzae and A. niger resemble the cellulose-hydrolysing enzymes of Myrothecium verrucaria (Whitaker, 1957) and of Stachybotry8 atra (Thomas, 1956) in having an endoglucosidase action pattern. This is supported by the evidence of Husemann & Lotterle (1950), who have shown by physical methods that the A. oryzae (Luitzym) preparation attacks cellulose in a random fashion characteristic of an endoglucosidase, and the appearance of a series of oligosaccharide intermediates during the hydrolysis of cellodextrins by the A. niger preparation suggests that it also possesses an endo-3-1:4-glucosidase (Stone, 1954).…”

Section: Comparison Of Components Hydrolysing P-1:4-gl0cosidic Linkagesmentioning

confidence: 99%

Fractionation of the β-glucosidases from Aspergillus niger

Murti

Stone

1961

Biochemical Journal

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“…In previous papers of this series it has been shown that Stachybotrys atra synthesizes at least three enzymes capable of hydrolysing ,B-glucosidic linkagesaryl ,B-glucosidase (Jermyn 1955), cellobiase (Youatt 1958), and cellulase (Thomas 1956). What is known of the specificity of these enzymes and their relationship to each other has been summarized elsewhere (Youatt and Jermyn 1959).…”

Section: Introductionmentioning

confidence: 99%

Fungal Cellulases XI. The Nature of the Inductive Process for Aryl ?-Glucosidase in Stachybotrys Atra

Ermyn¹

1965

Aust. Jnl. Of Bio. Sci.

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The properties of the inductive process for the aryl F/.glucosidase of S. atra are described. The induction appears to be independent of growth, respiration, and the uptake of measurable quantities of inducer into the cell. There is a lag period in the induction, the length of which depends on the physiological history of the mould and the temperature of induction; the temperature effect appears to be governed by a process with activation energy of 16 kcal/mole. The amount of inducible enzyme for a given sample of the mould appears to be equal to that which would have eventually been produced "constitutively" at the end of the growth period. The induction is inhibited competitively by monoses; this effect is reversed competitively by 3�0-methyl glucose. 3-0-Methyl glucose has a con-siderable inducer activity in its own right, and also stimulates the inductive effect due to thioglucoside. The only other inhibitors found are streptomycin and S-aminoethyl-L-cysteine. The effect of the latter is reversed by DL-lysine. No other substance known or expected to have an effect on cellular protein-synthesizing systems inhibited the induction.

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Ionospheric Recorders and Sporadic E

Cited by 12 publications

References 0 publications

The purification and properties of the C1 component of Trichoderma koningii cellulase

The purification and properties of the C1 component of Trichoderma koningii cellulase

Fractionation of the β-glucosidases from Aspergillus niger

Fungal Cellulases XI. The Nature of the Inductive Process for Aryl ?-Glucosidase in Stachybotrys Atra

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