Enzyme Cytochemistry of Fungi

Reiss, J.

doi:10.1016/s0079-6336(73)80001-4

Cited by 7 publications

(4 citation statements)

References 117 publications

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“…GOase, on the other hand, contains -<1% carbohydrate (16); thus, the continual release of GOase may indicate that the cell wall of D. dendroides has a very low degree of retention with respect to this protein. The absence of carbohydrate in GOase is interesting inasmuch as this conjugation is believed to be involved in the transport of proteins through the cell membrane (21).…”

Section: Discussionmentioning

confidence: 99%

Regulation of galactose oxidase synthesis and secretion in Dactylium dendroides: effects of pH and culture density

Shatzman¹,

Kosman²

1977

J Bacteriol

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The effects of pH and growth density on the amount of an extracellular enzyme, galactose oxidase, synthesized by the fungus Dactylium dendroides were studied. Growth at a pH below 6.7 caused a decrease in the ability of the organism to release galactose oxidase. The enzyme retained by these fungal cells was liberated whenever the pH was raised to 7.0. Cycloheximide addition failed to inhibit the appearance of this protein; [3H]leucine added prior to pH adjustment was not incorporated into the released protein. These observations indicate the released protein is not newly synthesized protein. The retained enzyme would be secreted slowly over a 2-day period if the pH was not increased. In addition to regulating protein retention, pH was also shown to be associated with vacuolization, cell volume, culture density, and inhibition of protein synthesis. Cultures maintained at low pH were characterized by a dense growth consisting of highly vacuolated, buoyant, fungal hyphae. Increasing the pH from 6 to 7 caused a decrease in vacuole size. Cells grown at neutral pH maintained a lower density of growth and, based on activity measurements, synthesized 33% more galactose oxidase. Furthermore, cultures grown at pH 6.0 and maintained at a lower cell density produced galactose oxidase at a level similar to that of cells grown at neutral pH. Thus, the elevated density of the cell culture was inhibitory to galactose oxidase synthesis. The observed effects on protein synthesis and release were rather specific for galactose oxidase, since other extracellular proteins appeared in the earliest stages of growth. celium as seen by phase-contrast microscopy. Volume increases and decreases are associated with 455 on August 3, 2020 by guest

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Section: Discussionmentioning

confidence: 99%

Regulation of galactose oxidase synthesis and secretion in Dactylium dendroides: effects of pH and culture density

Shatzman¹,

Kosman²

1977

J Bacteriol

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“…It is conceivable that the antimy cotic agent attaches itself near the active cen ter and thus impedes binding of the substrate and/or catalysis. As a result the cytotoxic agent, hydrogen peroxide [14], is not decom posed and thus causes irreversible fungal cell damages.…”

Section: Catalasementioning

confidence: 99%

Studies for the Elucidation of the Mode of Action of the Antimycotic Hydroxypyridone Compound, Rilopirox

Kruse¹,

Hengstenberg²,

Hänel³

et al. 1991

Pharmacology

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Rilopirox is a synthetic, fungicidal antimycotic agent with hydrophobic characteristics. Its chemical name is 6-[4-(4-chlorophenoxy)-phenoxymethyl]-1-hydroxy-4-methyl-2-pyridone and it has a molecular weight of 357.79. Rilopirox is very soluble in dimethyl sulfoxide (DMSO) and dimethylformamide (DMF) but poorly soluble in water. The amount of antimycotic agent remaining in the solution is dependent on the final concentration of the solvent and the amount of rilopirox used. Complexometric studies show that rilopirox has a high affinity for iron ions [unpubl. data]. Catalase, an iron-containing enzyme, is inhibited by the chelating agent rilopirox. Studies on yeast mitochondria and submitochondrial particles show that rilopirox inhibits the respiratory chain. Complex I (NADH-ubiquinone oxidoreductase) contains iron-sulfur proteins and is the main system which is inhibited.

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“…The crucial barrier in resistant crayfish seems to be located in the outer layers of the soft cuticle (Unestam and Weiss 1970), perhaps in the lipid epicuticle. Esterolytic activity can be important for animal pathogens (Reiss 1973), for fungal penetration through the waxy surface layer of plants (Nicholson et al 1972), and for hyphal penetration through the cuticle in insects (Zacharuk 1970).…”

Section: Discussionmentioning

confidence: 99%

Properties of Extracellular Enzymes from Aphanomyces astaci and Their Relevance in the Penetration Process of Crayfish Cuticle

Söderhäll¹,

Unestam²

1975

Physiologia Plantarum

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In culture filtrates from the crayfish plague parasite, Aphanomyces astaci, protease and a low level of hyaluronidase activity were found. The hyaluronidase activity was highest at pH 6.5 or above and at about 23X. The protease activity had a broad pH-optimum, between pH 7 and at least pH 10, and was partially denatured at 30°C. However, when incubated for 30 min with the substrate, casein, the activity increased logarithmically up to about 35-4O°C and had an apparent optimum at 45-50°C.The proteases from the parasitic as well as from two less proteolytic, saprophytic Aphanomyces species were predominantly constitutive and were excreted mainly by the older mycelia. Proteases from the parasite and a saprophyte did not reach full activity until 10-30 min after substrate addition.No lipase activity was found in the case of the mycelium of the parasitic species. However, esterase was apparently present inside germinating zoospores.The native enzymes of A. astaci could degrade freeze-dried soft cuticle from crayfish. The relevance of the different enzymes of A. astaci for the penetration process within the cuticle of crayfish is discussed.

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Enzyme Cytochemistry of Fungi

Cited by 7 publications

References 117 publications

Regulation of galactose oxidase synthesis and secretion in Dactylium dendroides: effects of pH and culture density

Regulation of galactose oxidase synthesis and secretion in Dactylium dendroides: effects of pH and culture density

Studies for the Elucidation of the Mode of Action of the Antimycotic Hydroxypyridone Compound, Rilopirox

Properties of Extracellular Enzymes from Aphanomyces astaci and Their Relevance in the Penetration Process of Crayfish Cuticle

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